|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
27-506 |
0e+00 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 939.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 27 LEVEFTKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRGSPWRRLDALGRGWLLHQLADL 106
Cdd:cd07141 2 PEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLADL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 107 VERDRAILATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLM 186
Cdd:cd07141 82 IERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 187 LVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVK 266
Cdd:cd07141 162 AAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 267 EAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDP 346
Cdd:cd07141 242 QAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 347 FDIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIE 426
Cdd:cd07141 322 FDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTID 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 427 EVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:cd07141 402 EVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
32-505 |
0e+00 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 832.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 32 TKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRGSpWRRLDALGRGWLLHQLADLVERDR 111
Cdd:cd07091 4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIERDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 112 AILATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKL 191
Cdd:cd07091 83 DELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 192 APALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASR 271
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 272 SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRT 351
Cdd:cd07091 243 SNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 352 EQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKR 431
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIER 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952740663 432 ANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07091 403 ANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
29-503 |
0e+00 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 684.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 29 VEFTKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRGsPWRRLDALGRGWLLHQLADLVE 108
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 109 RDRAILATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLV 188
Cdd:cd07142 80 KHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 189 WKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEA 268
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 269 ASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFD 348
Cdd:cd07142 240 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 349 IRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEV 428
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952740663 429 IKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
32-507 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 673.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 32 TKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQrgsPWRRLDALGRGWLLHQLADLVERDR 111
Cdd:COG1012 6 YPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 112 AILATLETMDTGKPFLHAFFiDLEGCIKTLRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWK 190
Cdd:COG1012 83 EELAALLTLETGKPLAEARG-EVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 191 LAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAAS 270
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 271 RsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIR 350
Cdd:COG1012 242 E-NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 351 TEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMED-RGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVI 429
Cdd:COG1012 321 TDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952740663 430 KRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIY-AQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
32-507 |
0e+00 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 669.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 32 TKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQrgSPWRR-LDALGRGWLLHQLADLVERD 110
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWGLkVSGSKRGRCLSKLADLMERN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 111 RAILATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWK 190
Cdd:cd07143 85 LDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 191 LAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAAS 270
Cdd:cd07143 165 IAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 271 RSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIR 350
Cdd:cd07143 245 KSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 351 TEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIK 430
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIK 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952740663 431 RANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07143 405 RANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
45-503 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 659.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 45 SGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQrgsPWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGK 124
Cdd:pfam00171 5 ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELETLENGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 125 PFLHAFFiDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVK 204
Cdd:pfam00171 82 PLAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 205 PAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGK 284
Cdd:pfam00171 161 PSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTLELGGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 285 NPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDK 364
Cdd:pfam00171 240 NPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 365 ILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVF 444
Cdd:pfam00171 320 VLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVF 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 445 TKNLDKALKLASALESGTVWINCYNAIYA-QAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:pfam00171 400 TSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
26-509 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 656.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 26 SLEVEFTKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRGsPWRRLDALGRGWLLHQLAD 105
Cdd:PLN02466 52 PVQVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEG-PWPKMTAYERSRILLRFAD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 106 LVERDRAILATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLL 185
Cdd:PLN02466 131 LLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 186 MLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLV 265
Cdd:PLN02466 211 MFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 266 KEAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGD 345
Cdd:PLN02466 291 LELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 346 PFDIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNI 425
Cdd:PLN02466 371 PFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 426 EEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:PLN02466 451 DEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVT 530
|
....
gi 1952740663 506 KLDD 509
Cdd:PLN02466 531 PLKN 534
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
32-507 |
0e+00 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 653.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 32 TKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQrgSPWRRLDALGRGWLLHQLADLVERDR 111
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEKNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 112 AILATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKL 191
Cdd:cd07144 86 DLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 192 APALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASr 271
Cdd:cd07144 166 APALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 272 SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKR-PIGDPFDIR 350
Cdd:cd07144 245 QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 351 TEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMED---RGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEE 427
Cdd:cd07144 325 TVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEglgKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 428 VIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07144 405 AIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHINL 484
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
72-505 |
0e+00 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 616.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 72 DKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPfLHAFFIDLEGCIKTLRYFAGWADKI 151
Cdd:cd07078 1 DAAVAAARAAFKA---WAALPPAERAAILRKLADLLEERREELAALETLETGKP-IEEALGEVARAADTFRYYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 152 QGRTIPTDD-NVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVV 230
Cdd:cd07078 77 HGEVIPSPDpGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 231 NIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQ 310
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 311 GQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAME-DR 389
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEgGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 390 GLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYN 469
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 1952740663 470 A-IYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07078 396 VgAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
35-508 |
0e+00 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 600.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 35 FINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRGsPWRRLDALGRGWLLHQLADLVERDRAIL 114
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSG-EWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 115 ATLETMDTGKPFLHAFfIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPA 194
Cdd:cd07119 80 ARLETLNTGKTLRESE-IDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 195 LCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsNL 274
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 275 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQG 354
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 355 PQIDQKQFDKILDLIESGKKEGAKLECGGSAMED----RGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIK 430
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952740663 431 RANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLD 508
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININLS 475
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
28-512 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 598.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 28 EVEFTKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRGsPWRRLDALGRGWLLHQLADLV 107
Cdd:PLN02766 17 EIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 108 ERDRAILATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLML 187
Cdd:PLN02766 96 EEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 188 VWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKE 267
Cdd:PLN02766 176 FMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 268 AASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPF 347
Cdd:PLN02766 256 AAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 348 DIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEE 427
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 428 VIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPL 495
|
....*
gi 1952740663 508 DDkSP 512
Cdd:PLN02766 496 YN-SP 499
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
46-505 |
0e+00 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 583.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 46 GKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRGSpWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKP 125
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 126 FLHAFFIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKP 205
Cdd:cd07112 80 ISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 206 AEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGKN 285
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 286 PCIVCADA-DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDK 364
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 365 ILDLIESGKKEGAKLECGGSA--MEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAA 442
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952740663 443 VFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
51-505 |
0e+00 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 579.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 51 TYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFqRGSPWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPfLHAF 130
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAF-EGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKL-IRET 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 131 FIDLEGCIKTLRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQT 209
Cdd:cd07114 79 RAQVRYLAEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 210 PLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIV 289
Cdd:cd07114 159 PASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 290 CADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLI 369
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 370 ESGKKEGAKLECGGSAME----DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFT 445
Cdd:cd07114 318 ARAREEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWT 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 446 KNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07114 398 RDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
51-505 |
0e+00 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 568.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 51 TYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAF 130
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG---WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 131 FIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTP 210
Cdd:cd07093 78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 211 LTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVC 290
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 291 ADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIE 370
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 371 SGKKEGAKLECGGSAME----DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTK 446
Cdd:cd07093 317 LARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952740663 447 NLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
51-507 |
0e+00 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 565.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 51 TYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQrgsPWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAF 130
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 131 FIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTP 210
Cdd:cd07115 78 RLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 211 LTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCIVC 290
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 291 ADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIE 370
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 371 SGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDK 450
Cdd:cd07115 317 VGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952740663 451 ALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
32-506 |
0e+00 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 559.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 32 TKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRGsPWRRLDALGRGWLLHQLADLVERDR 111
Cdd:cd07140 6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENG-EWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 112 AILATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADKIQGRTIPTD----DNVVCFTRHEPIGVCGAITPWNFPLLML 187
Cdd:cd07140 85 EELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNYPLMML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 188 VWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKE 267
Cdd:cd07140 165 AWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 268 AASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPF 347
Cdd:cd07140 245 SCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 348 DIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKN--I 425
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 426 EEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07140 405 DGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTI 484
|
.
gi 1952740663 506 K 506
Cdd:cd07140 485 E 485
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
52-505 |
0e+00 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 529.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 52 YNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFf 131
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 132 IDLEGCIKTLRYFAGWADKIQGRTIPTDD-NVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTP 210
Cdd:cd07103 78 GEVDYAASFLEWFAEEARRIYGRTIPSPApGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 211 LTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCIVC 290
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPFIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 291 ADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIE 370
Cdd:cd07103 237 DDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 371 SGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDK 450
Cdd:cd07103 317 DAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1952740663 451 ALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07103 397 AWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
33-507 |
0e+00 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 524.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 33 KIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRA 112
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT---WGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 113 ILATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLA 192
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 193 PALCCGNTIVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRs 272
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 273 NLKRVTLELGGKNPCIVCADA-----DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPF 347
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 348 DIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGG----SAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFK 423
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGerltLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 424 NIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476
|
....
gi 1952740663 504 TIKL 507
Cdd:cd07559 477 LVSY 480
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
34-504 |
4.37e-179 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 511.28 E-value: 4.37e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 34 IFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAF---QRGSPWRRLDalgrgwLLHQLADLVERD 110
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFpawSATSVEERAA------LLERIAEAYEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 111 RAILATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVcftrHEPIGVCGAITPWNFPLLMLVWK 190
Cdd:cd07138 75 ADELAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEFEERRGNSLVV----REPIGVCGLITPWNWPLNQIVLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 191 LAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAAS 270
Cdd:cd07138 151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 271 RSnLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIR 350
Cdd:cd07138 231 DT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 351 TEQGPQIDQKQFDKILDLIESGKKEGAKLECGGS---AMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEE 427
Cdd:cd07138 310 TTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDE 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952740663 428 VIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINcYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07138 390 AIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
35-509 |
1.28e-178 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 510.96 E-value: 1.28e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 35 FINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLV-ERDRAi 113
Cdd:PRK13252 10 YIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVDILrERNDE- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 114 LATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAP 193
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 194 ALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPtVGAAISSHPHISKIAFTGSTEVGKLVKEAASRSn 273
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 274 LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQ 353
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 354 GPQIDQKQFDKILDLIESGKKEGAKLECGGSAME----DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVI 429
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTeggfANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 430 KRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLDD 509
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVEMGP 483
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
52-505 |
2.86e-177 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 505.91 E-value: 2.86e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 52 YNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFF 131
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG---WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 132 iDLEGCIKTLRYFAGWAdkIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPL 211
Cdd:cd07106 79 -EVGGAVAWLRYTASLD--LPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 212 TALYLGSLIKEVgFPPGVVNIVPGfGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCIVCA 291
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAA-KTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 292 DADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIES 371
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 372 GKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKA 451
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1952740663 452 LKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
51-503 |
1.57e-176 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 504.15 E-value: 1.57e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 51 TYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAF 130
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 131 fIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTP 210
Cdd:cd07090 78 -VDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 211 LTALYLGSLIKEVGFPPGVVNIVPGFGPTvGAAISSHPHISKIAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCIVC 290
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 291 ADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIE 370
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 371 SGKKEGAKLECGGS--AMED---RGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFT 445
Cdd:cd07090 315 SAKQEGAKVLCGGErvVPEDgleNGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952740663 446 KNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
65-505 |
2.26e-173 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 496.09 E-value: 2.26e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 65 EGDKLDVDKAVEAAHAAFQRGsPWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFFiDLEGCIKTLRYF 144
Cdd:cd07118 15 EGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG-EIEGAADLWRYA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 145 AGWADKIQGRTIPT-DDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEV 223
Cdd:cd07118 93 ASLARTLHGDSYNNlGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 224 GFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAH 303
Cdd:cd07118 173 GLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFADADLDAAADAVV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 304 QGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGG 383
Cdd:cd07118 252 FGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 384 SAMEDR-GLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGT 462
Cdd:cd07118 332 ERLASAaGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGT 411
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1952740663 463 VWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07118 412 VWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
35-501 |
1.05e-172 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 495.10 E-value: 1.05e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 35 FINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAIL 114
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGE---WAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 115 ATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPA 194
Cdd:TIGR01804 78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 195 LCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASrSNL 274
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 275 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQG 354
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 355 PQIDQKQFDKILDLIESGKKEGAKLECGGSAME----DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIK 430
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPEnvglQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952740663 431 RANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVK 501
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
33-507 |
1.44e-172 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 495.05 E-value: 1.44e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 33 KIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRA 112
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT---WRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 113 ILATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLA 192
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 193 PALCCGNTIVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRs 272
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 273 NLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTE 352
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 353 QGPQIDQKQFDKILDLIESGKKEGAKLECGG----SAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEV 428
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGhrltENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952740663 429 IKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
51-504 |
3.70e-172 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 493.02 E-value: 3.70e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 51 TYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPfLHAF 130
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR---WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKP-LDEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 131 FIDLEGCIKTLRYFAGWADKI---QGRTIPTDDN-VVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPA 206
Cdd:cd07110 77 AWDVDDVAGCFEYYADLAEQLdakAERAVPLPSEdFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 207 EQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNP 286
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 287 CIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKIL 366
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 367 DLIESGKKEGAKLECGGSAME--DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVF 444
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 445 TKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
76-505 |
4.35e-172 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 489.43 E-value: 4.35e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 76 EAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPfLHAFFIDLEGCIKTLRYFAGWADKIQGRT 155
Cdd:cd06534 1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKP-IEEALGEVARAIDTFRYAAGLADKLGGPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 156 IP-TDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVP 234
Cdd:cd06534 77 LPsPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 235 GFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCC 314
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 315 TAASRVFVEEQIYPEFVRRSVeyakkrpigdpfdirteqgpqidqkqfdkildliesgkkegaklecggsamedrglfik 394
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 395 pTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIY-A 473
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVgP 335
|
410 420 430
....*....|....*....|....*....|..
gi 1952740663 474 QAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
35-505 |
1.23e-168 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 484.46 E-value: 1.23e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 35 FINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAfQRGspWRRLDALGRGWLLHQLADLVERDRAIL 114
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAA-QKA--WERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 115 ATLETMDTGKPFLHAFfIDLEGCIKTLRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAP 193
Cdd:cd07088 78 AKLIVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDrPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 194 ALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsN 273
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-N 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 274 LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQ 353
Cdd:cd07088 236 ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 354 GPQIDQKQFDKILDLIESGKKEGAKLECGGSAME-DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRA 432
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952740663 433 NSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
52-505 |
7.68e-168 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 482.12 E-value: 7.68e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 52 YNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRGspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFf 131
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESG--WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 132 IDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPL 211
Cdd:cd07109 79 ADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 212 TALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCA 291
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 292 DADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDiRTEQGPQIDQKQFDKILDLIES 371
Cdd:cd07109 238 DADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 372 GKKEGAKLECGGSAMEDR---GLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNL 448
Cdd:cd07109 317 ARARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 449 DKALKLASALESGTVWINCYNA---IyaQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07109 397 DRALRVARRLRAGQVFVNNYGAgggI--ELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
52-505 |
4.13e-167 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 480.29 E-value: 4.13e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 52 YNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFF 131
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPS---WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 132 IDLEGCIKTLRYFAGWADKIQGRT----IPtddNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAE 207
Cdd:cd07092 79 DELPGAVDNFRFFAGAARTLEGPAageyLP---GHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 208 QTPLTALYLGSLIKEVgFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPC 287
Cdd:cd07092 156 TTPLTTLLLAELAAEV-LPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD-TLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILD 367
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 368 LIEsGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKN 447
Cdd:cd07092 314 FVE-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952740663 448 LDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
35-503 |
3.15e-166 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 478.67 E-value: 3.15e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 35 FINNEWHESKSGKkfATYNPSTL-EKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAI 113
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSDTsDVVGKYARASAEDADAAIAAAAAAFPA---WRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 114 LATLETMDTGKPFLHAFFiDLEGCIKTLRYFAGWADKIQGRTIP-TDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLA 192
Cdd:cd07097 79 LARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 193 PALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASrS 272
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-A 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 273 NLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTE 352
Cdd:cd07097 237 RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 353 QGPQIDQKQFDKILDLIESGKKEGAKLECGGSA--MEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIK 430
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKLVYGGERlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952740663 431 RANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYA-QAPFGGFKMSGNG-RELGEYALAEYTEVKTV 503
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDyHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
31-507 |
1.27e-163 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 472.09 E-value: 1.27e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 31 FTKIFINNEWhESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERD 110
Cdd:PRK13473 2 QTKLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE---WSQTTPKERAEALLKLADAIEEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 111 RAILATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADKIQGRTipTDDNVVCFT---RHEPIGVCGAITPWNFPLLML 187
Cdd:PRK13473 78 ADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKA--AGEYLEGHTsmiRRDPVGVVASIAPWNYPLMMA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 188 VWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKE 267
Cdd:PRK13473 156 AWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 268 AASRSnLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPF 347
Cdd:PRK13473 235 AAADS-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 348 DIRTEQGPQIDQKQFDKILDLIESGKKEG-AKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIE 426
Cdd:PRK13473 314 DEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 427 EVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:PRK13473 394 QAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVK 473
|
.
gi 1952740663 507 L 507
Cdd:PRK13473 474 H 474
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
51-507 |
3.23e-163 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 470.32 E-value: 3.23e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 51 TYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPfLHAF 130
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE---WRATTPLERARMLRELATRLREHAEELALIDALDCGNP-VSAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 131 FIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTP 210
Cdd:cd07107 77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 211 LTALYLGSLIKEVgFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRSnLKRVTLELGGKNPCIVC 290
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 291 ADADLDLAVECAHQGVFFN-QGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLI 369
Cdd:cd07107 235 PDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 370 ESGKKEGAKLECGGSAMED----RGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFT 445
Cdd:cd07107 315 DSAKREGARLVTGGGRPEGpaleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952740663 446 KNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
19-504 |
1.39e-162 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 470.75 E-value: 1.39e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 19 ALPRPVRSLeveftkiFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQR--GSPWRRLDALGR 96
Cdd:PLN02467 2 AIPVPRRQL-------FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkGKDWARTTGAVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 97 GWLLHQLADLVERDRAILATLETMDTGKPFLHAFF--IDLEGCIKtlrYFAGWADKIQGR-----TIPtDDNVVCFTRHE 169
Cdd:PLN02467 75 AKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWdmDDVAGCFE---YYADLAEALDAKqkapvSLP-METFKGYVLKE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 170 PIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPH 249
Cdd:PLN02467 151 PLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 250 ISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPE 329
Cdd:PLN02467 231 VDKIAFTGSTATGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 330 FVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMED--RGLFIKPTVFSEVTDTMRI 407
Cdd:PLN02467 310 FLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 408 AKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGR 487
Cdd:PLN02467 390 WREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGR 469
|
490
....*....|....*..
gi 1952740663 488 ELGEYALAEYTEVKTVT 504
Cdd:PLN02467 470 ELGEWGLENYLSVKQVT 486
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
35-505 |
3.30e-162 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 468.75 E-value: 3.30e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 35 FINNEWHESKSGKKFATYNPSTLEKIC-EVEEGDKLDVDKAVEAAHAAFqrgSPWRRLDALGRGWLLHQLADLVERDRAI 113
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVVgTFPLSTASDVDAAVEAAREAF---PEWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 114 LATLETMDTGKPFLHAFfIDLEGCIKTLRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLA 192
Cdd:cd07131 79 LARLVTREMGKPLAEGR-GDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 193 PALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRS 272
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 273 NlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTE 352
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 353 QGPQIDQKQFDKILDLIESGKKEGAKLECGGSAME----DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEV 428
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTgggyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 429 IKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNAiYAQAPFGGFKMSGNG-RELGEYALAEYTEVKTVTI 505
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNapTIGA-EVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
70-505 |
5.36e-160 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 461.23 E-value: 5.36e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 70 DVDKAVEAAHAAFQrgsPWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFFiDLEGCIKTLRYFAGWAD 149
Cdd:cd07104 1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAF-EVGAAIAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 150 KIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLT-ALYLGSLIKEVGFPP 227
Cdd:cd07104 77 RPEGEILPSDvPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 228 GVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVF 307
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 308 FNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAme 387
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 388 dRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINC 467
Cdd:cd07104 314 -EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 1952740663 468 YNAI-YAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07104 393 QTVNdEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
52-503 |
1.68e-159 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 460.94 E-value: 1.68e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 52 YNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRGsPWRRlDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFF 131
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTG-DWST-DAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 132 IDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVC-----FTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPA 206
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFPWEFDLPVPALRGgpgrrVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 207 EQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNP 286
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 287 CIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKIL 366
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 367 DLIESGKKEGAKLECGGSAME--DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVF 444
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAglDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952740663 445 TKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
53-505 |
1.20e-157 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 456.44 E-value: 1.20e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 53 NPSTLEKICEVEEGDKLDVDKAVEAAHAAFQrgsPWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFFI 132
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 133 DLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLT 212
Cdd:cd07108 80 EAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 213 ALYLGSLIKEVgFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLV-KEAASRsnLKRVTLELGGKNPCIVCA 291
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIyRAAADR--LIPVSLELGGKSPMIVFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 292 DADLDLAVECAHQGV-FFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIE 370
Cdd:cd07108 237 DADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 371 SGKKE-GAKLECGGSAMED----RGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFT 445
Cdd:cd07108 317 LGLSTsGATVLRGGPLPGEgplaDGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952740663 446 KNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELG-EYALAEYTEVKTVTI 505
Cdd:cd07108 397 RDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
34-505 |
1.76e-155 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 451.26 E-value: 1.76e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 34 IFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRGsPWRRLDALGRGWLLHQLADLVERDRAI 113
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 114 LATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADK---IQGRTIPTDDNVVcfTRHEPIGVCGAITPWNFPLLMLVWK 190
Cdd:cd07139 80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDfpfEERRPGSGGGHVL--VRREPVGVVAAIVPWNAPLFLAALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 191 LAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGfGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAAS 270
Cdd:cd07139 158 IAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 271 RsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIR 350
Cdd:cd07139 237 E-RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 351 TEQGPQIDQKQFDKILDLIESGKKEGAKLECGGS--AMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEV 428
Cdd:cd07139 316 TQIGPLASARQRERVEGYIAKGRAEGARLVTGGGrpAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952740663 429 IKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYnAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07139 396 VRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
49-505 |
1.26e-153 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 445.62 E-value: 1.26e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 49 FATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQrgsPWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLH 128
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 129 AFFiDLEGCIKTLRYFAGWADKIQGRTIPTDDN-VVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAE 207
Cdd:cd07150 78 AWF-ETTFTPELLRAAAGECRRVRGETLPSDSPgTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 208 QTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPC 287
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILD 367
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 368 LIESGKKEGAKLECGGsamEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKN 447
Cdd:cd07150 316 QVEDAVAKGAKLLTGG---KYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 448 LDKALKLASALESGTVWINCyNAIY--AQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07150 393 LQRAFKLAERLESGMVHIND-PTILdeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
35-497 |
9.39e-153 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 444.53 E-value: 9.39e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 35 FINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAIL 114
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES---WSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 115 ATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADKIQgrtipTDdnvvcFTRHEPIGVCGAITPWNFPLLMLVWKLAPA 194
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLD-----TE-----LAGWKPVGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 195 LCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGfGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRSNl 274
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTG-NGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTG- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 275 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQG 354
Cdd:cd07111 250 KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 355 PQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANS 434
Cdd:cd07111 330 AIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANN 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952740663 435 LEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEY 497
Cdd:cd07111 410 TPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
25-508 |
5.32e-151 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 440.87 E-value: 5.32e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 25 RSLEVEfTKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRGSpWRRLDALGRGWLLHQLA 104
Cdd:PRK09847 14 LSLAIE-NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 105 DLVERDRAILATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPL 184
Cdd:PRK09847 92 DLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 185 LMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKL 264
Cdd:PRK09847 172 LLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 265 VKEAASRSNLKRVTLELGGKNPCIVCADA-DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPI 343
Cdd:PRK09847 252 LLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 344 GDPFDIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAmeDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFK 423
Cdd:PRK09847 332 GHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNA--GLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 424 NIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:PRK09847 410 SEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
....*
gi 1952740663 504 TIKLD 508
Cdd:PRK09847 490 WISLE 494
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
15-503 |
7.47e-151 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 440.67 E-value: 7.47e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 15 RKPPALPRPVRSLEVEFTKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQrgsPWRRLDAL 94
Cdd:PLN02278 8 MDAQSALVKLRNAGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLTAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 95 GRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFfIDLEGCIKTLRYFAGWADKIQGRTIPTDD-NVVCFTRHEPIGV 173
Cdd:PLN02278 85 ERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAI-GEVAYGASFLEYFAEEAKRVYGDIIPSPFpDRRLLVLKQPVGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 174 CGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKI 253
Cdd:PLN02278 164 VGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 254 AFTGSTEVGKLVKEAASRSnLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRR 333
Cdd:PLN02278 244 TFTGSTAVGKKLMAGAAAT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 334 SVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIF 413
Cdd:PLN02278 323 FSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 414 GPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYA 493
Cdd:PLN02278 403 GPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYG 482
|
490
....*....|
gi 1952740663 494 LAEYTEVKTV 503
Cdd:PLN02278 483 IDEYLEIKYV 492
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
35-506 |
2.71e-148 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 433.02 E-value: 2.71e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 35 FINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQrgSPWRRLDALGRGWLLHQLADLVERDRAIL 114
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 115 ATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADKIQGRTI------PTDDNVVCFTRHEPIGVCGAITPWNFPLLMLV 188
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLapsipsMQGERYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 189 WKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGpTVGAAISSHPHISKIAFTGSTEVGKLVKEA 268
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 269 ASrSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFD 348
Cdd:cd07113 240 AA-SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 349 IRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEV 428
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952740663 429 IKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
52-505 |
2.33e-147 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 429.71 E-value: 2.33e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 52 YNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRGspwRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPfLHAFF 131
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKP-IKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 132 IDLEGCIKTLRYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPA 206
Cdd:cd07149 80 KEVDRAIETLRLSAEEAKRLAGETIPFDaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 207 EQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASrsnLKRVTLELGGKNP 286
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGSNAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 287 CIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKIL 366
Cdd:cd07149 237 VIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 367 DLIESGKKEGAKLECGGSAmedRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTK 446
Cdd:cd07149 317 EWVEEAVEGGARLLTGGKR---DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTN 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 447 NLDKALKLASALESGTVWIN-CYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07149 394 DLQKALKAARELEVGGVMINdSSTFRVDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
49-505 |
4.26e-147 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 429.46 E-value: 4.26e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 49 FATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLH 128
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV---MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 129 AFfIDLEGCIKTLRYFAGWADKIQGRTIPTDD-----NVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVV 203
Cdd:cd07145 78 SR-VEVERTIRLFKLAAEEAKVLRGETIPVDAyeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 204 KPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLV-KEAASRsnLKRVTLELG 282
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIaSKAGGT--GKKVALELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 283 GKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQF 362
Cdd:cd07145 235 GSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 363 DKILDLIESGKKEGAKLECGGSAMEdrGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAA 442
Cdd:cd07145 315 ERMENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQAS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952740663 443 VFTKNLDKALKLASALESGTVWINCYNAI-YAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07145 393 VFTNDINRALKVARELEAGGVVINDSTRFrWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
35-505 |
8.47e-146 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 426.98 E-value: 8.47e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 35 FINNEWHESkSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAIL 114
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE---WRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 115 ATLETMDTGKPFLHAF-----FIDLegCIktlrYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLV 188
Cdd:cd07086 78 GRLVSLEMGKILPEGLgevqeMIDI--CD----YAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 189 WKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEV----GFPPGVVNIVPGFGPtVGAAISSHPHISKIAFTGSTEVGKL 264
Cdd:cd07086 152 WNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 265 VKEAASRSNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIG 344
Cdd:cd07086 231 VGETVARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 345 DPFDIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAME--DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKF 422
Cdd:cd07086 310 DPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDggEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 423 KNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALES--GTVWIN--CYNAiYAQAPFGGFKMSGNGRELGEYALAEYT 498
Cdd:cd07086 390 DSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSdcGIVNVNipTSGA-EIGGAFGGEKETGGGRESGSDAWKQYM 468
|
....*..
gi 1952740663 499 EVKTVTI 505
Cdd:cd07086 469 RRSTCTI 475
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
35-505 |
1.96e-140 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 413.39 E-value: 1.96e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 35 FINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAIL 114
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA---WGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 115 ATLETMDTGKPFLHAFFIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPA 194
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 195 LCCGNTIVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsNL 274
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 275 KRVTLELGGKNPCIVCA------DADLDLAVECAhqGVF-FNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPF 347
Cdd:cd07116 239 IPVTLELGGKSPNIFFAdvmdadDAFFDKALEGF--VMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 348 DIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGL----FIKPTVFSEvTDTMRIAKEEIFGPVQPILKFK 423
Cdd:cd07116 317 DTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 424 NIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07116 396 DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNL 475
|
..
gi 1952740663 504 TI 505
Cdd:cd07116 476 LV 477
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
34-504 |
1.83e-139 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 412.00 E-value: 1.83e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 34 IFINNEwhESKSGKKFATYNPS-TLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRA 112
Cdd:cd07124 35 LVIGGK--EVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPT---WRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 113 ILATLETMDTGKPFLHAFfIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLA 192
Cdd:cd07124 110 ELAAWMVLEVGKNWAEAD-ADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 193 PALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASR- 271
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 272 ----SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPF 347
Cdd:cd07124 269 qpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 348 DIRTEQGPQIDQKQFDKILDLIESGKKEGaKLECGGSAMED--RGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNI 425
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 426 EEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNAIYAQAPFGGFKMSG-NGRELGEYALAEYTEVKT 502
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGtGSKAGGPDYLLQFMQPKT 507
|
..
gi 1952740663 503 VT 504
Cdd:cd07124 508 VT 509
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
35-507 |
1.49e-138 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 408.34 E-value: 1.49e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 35 FINNEWHESksGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAfQRGsPWRRLDALGRGWLLHQLADLVERDRAIL 114
Cdd:TIGR03216 4 FINGAFVES--GKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAA-LKG-PWGKMTVAERADLLYAVADEIERRFDDF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 115 ATLETMDTGKPFLHAFFIDLEGCIKTLRYFAgwaDKIqgRTIPTD---------DNVVCFTRHEPIGVCGAITPWNFPLL 185
Cdd:TIGR03216 80 LAAEVADTGKPRSLASHLDIPRGAANFRVFA---DVV--KNAPTEcfematpdgKGALNYAVRKPLGVVGVISPWNLPLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 186 MLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGP-TVGAAISSHPHISKIAFTGSTEVGKL 264
Cdd:TIGR03216 155 LMTWKVGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPdSAGEFLTRHPGVDAITFTGETRTGSA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 265 VKEAASRSnLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIG 344
Cdd:TIGR03216 235 IMKAAADG-VKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 345 DPFDIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGG-----SAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPI 419
Cdd:TIGR03216 314 VPDDPATNMGPLISAEHRDKVLSYYALAVEEGATVVTGGgvpdfGDALAGGAWVQPTIWTGLPDSARVVTEEIFGPCCHI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 420 LKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTE 499
Cdd:TIGR03216 394 APFDSEEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYTE 473
|
....*...
gi 1952740663 500 VKTVTIKL 507
Cdd:TIGR03216 474 LTNVCIKL 481
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
38-506 |
1.43e-134 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 397.83 E-value: 1.43e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 38 NEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAfQRgsPWRRLDALGRGWLLHQLADLVERDRAILATL 117
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA-QK--EWAATLPQERAEILEKAAQILEERRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 118 ETMDTGKPFLHAFfIDLEGCIKTLRYFAGWADKIQGRTIPTD----DNVVcftRHEPIGVCGAITPWNFPLLMLVWKLAP 193
Cdd:cd07151 78 LIRESGSTRIKAN-IEWGAAMAITREAATFPLRMEGRILPSDvpgkENRV---YREPLGVVGVISPWNFPLHLSMRSVAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 194 ALCCGNTIVVKPAEQTPLTA-LYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRs 272
Cdd:cd07151 154 ALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 273 NLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTE 352
Cdd:cd07151 233 HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 353 QGPQIDQKQFDKILDLIESGKKEGAKLECGGSAmedRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRA 432
Cdd:cd07151 313 VGPLINESQVDGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELA 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952740663 433 NSLEYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNAiYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:cd07151 390 NDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINdqPVND-EPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
51-504 |
5.38e-133 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 393.25 E-value: 5.38e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 51 TYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFqRGSPWRRlDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAF 130
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAF-DETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 131 FiDLEGCIKTLRYFAGWADKIQGRTI-PTDDNVVCFTRhEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQT 209
Cdd:cd07120 79 F-EISGAISELRYYAGLARTEAGRMIePEPGSFSLVLR-EPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 210 PLTALYLGSLIKEV-GFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCI 288
Cdd:cd07120 157 AQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTPCI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 289 VCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDL 368
Cdd:cd07120 236 VFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 369 IESGKKEGAK-LECGGSAMED--RGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFT 445
Cdd:cd07120 316 VERAIAAGAEvVLRGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952740663 446 KNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07120 396 RDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
52-501 |
9.16e-132 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 389.87 E-value: 9.16e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 52 YNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAff 131
Cdd:TIGR01780 2 YNPATGEIIGSVPDQGVDETEAAIRAAYEAFKT---WRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 132 idlEGCIKT----LRYFAGWADKIQGRTIPT--DDNVVCFTRhEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKP 205
Cdd:TIGR01780 77 ---KGEILYaasfLEWFAEEAKRVYGDTIPSpqSDKRLIVIK-QPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 206 AEQTPLTALYLGSLIKEVGFPPGVVNIVPG-FGPTVGAAISSHPHISKIAFTGSTEVGK-LVKEAAsrSNLKRVTLELGG 283
Cdd:TIGR01780 153 AEQTPLSALALARLAEQAGIPKGVLNVITGsRAKEVGNVLTTSPLVRKISFTGSTNVGKiLMKQSA--STVKKVSMELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 284 KNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFD 363
Cdd:TIGR01780 231 NAPFIVFDDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 364 KILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAV 443
Cdd:TIGR01780 311 KVEKHIADAVEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYF 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952740663 444 FTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVK 501
Cdd:TIGR01780 391 FSRDLSRIWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
33-506 |
2.39e-131 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 389.62 E-value: 2.39e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 33 KIFINNEWHESkSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQ----RGSPWRRLDalgrgwLLHQLADLVE 108
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRgwwpTMPLEERID------CLHKFADLLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 109 RDRAILATLETMDTGKPFLHAFfIDLEGCIKTLRYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFP 183
Cdd:cd07082 76 ENKEEVANLLMWEIGKTLKDAL-KEVDRTIDYIRDTIEELKRLDGDSLPGDwfpgtKGKIAQVRREPLGVVLAIGPFNYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 184 LLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGK 263
Cdd:cd07082 155 LNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 264 LVKEAASRsnlKRVTLELGGKNPCIVCADADLDLAV-ECAHQGVFFNqGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRP 342
Cdd:cd07082 235 RLKKQHPM---KRLVLELGGKDPAIVLPDADLELAAkEIVKGALSYS-GQRCTAIKRVLVHESVADELVELLKEEVAKLK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 343 IGDPFDIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEdrGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKF 422
Cdd:cd07082 311 VGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG--GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 423 KNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNA----IYaqaPFGGFKMSGNGRELGEYALAEYT 498
Cdd:cd07082 389 NDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQrgpdHF---PFLGRKDSGIGTQGIGDALRSMT 465
|
....*...
gi 1952740663 499 EVKTVTIK 506
Cdd:cd07082 466 RRKGIVIN 473
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
71-505 |
7.45e-131 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 386.82 E-value: 7.45e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 71 VDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFF-IDLegCIKTLRYFAGWAD 149
Cdd:cd07100 1 IEAALDRAHAAFLA---WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAeVEK--CAWICRYYAENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 150 K-IQGRTIPTDDNVvCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPG 228
Cdd:cd07100 76 AfLADEPIETDAGK-AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 229 VVNIVPGFGPTVGAAISsHPHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFF 308
Cdd:cd07100 155 VFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 309 NQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMED 388
Cdd:cd07100 233 NAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 389 RGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCY 468
Cdd:cd07100 313 PGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGM 392
|
410 420 430
....*....|....*....|....*....|....*..
gi 1952740663 469 NAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07100 393 VKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
53-505 |
4.32e-129 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 383.32 E-value: 4.32e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 53 NPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFfI 132
Cdd:cd07094 5 NPYDGEVIGKVPADDRADAEEALATARAGAEN---RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR-V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 133 DLEGCIKTLRYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAE 207
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 208 QTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASrsnLKRVTLELGGKNPC 287
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILD 367
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 368 LIESGKKEGAKLECGGsamEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKN 447
Cdd:cd07094 318 WVEEAVEAGARLLCGG---ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952740663 448 LDKALKLASALESGTVWINCYNAIYAQA-PFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07094 395 LNVAFKAAEKLEVGGVMVNDSSAFRTDWmPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
70-505 |
9.46e-129 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 381.54 E-value: 9.46e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 70 DVDKAVEAAHAAFQrgsPWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFFiDLEGCIKTLRYFAGWAD 149
Cdd:cd07105 1 DADQAVEAAAAAFP---AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGF-NVDLAAGMLREAASLIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 150 KIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPG 228
Cdd:cd07105 77 QIIGGSIPSDkPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 229 VVNIV---PGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQG 305
Cdd:cd07105 157 VLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAALFG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 306 VFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDpfdirTEQGPQIDQKQFDKILDLIESGKKEGAKLECGG-S 384
Cdd:cd07105 236 AFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGlA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 385 AMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVW 464
Cdd:cd07105 311 DESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVH 390
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1952740663 465 INCYNaIY--AQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07105 391 INGMT-VHdePTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
58-505 |
8.15e-128 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 379.72 E-value: 8.15e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 58 EKICEVEEGDKLDVDKAVEAAHAAfQRGspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFFiDLEGC 137
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAA-QRA--WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGF-EVGAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 138 IKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTA-LYL 216
Cdd:cd07152 78 IGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 217 GSLIKEVGFPPGVVNIVPGfGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLD 296
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 297 LAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIESGKKEG 376
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 377 AKLECGGSAmedRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLAS 456
Cdd:cd07152 316 ARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1952740663 457 ALESGTVWINCYNAIY-AQAPFGGFKMSGNGRELGEYA-LAEYTEVKTVTI 505
Cdd:cd07152 393 RLRTGMLHINDQTVNDePHNPFGGMGASGNGSRFGGPAnWEEFTQWQWVTV 443
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
52-505 |
1.65e-126 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 376.56 E-value: 1.65e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 52 YNPSTLEKICEVEEGDKLDVDKAVEAAHAAfQRGspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPfLHAFF 131
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAA-QRA--WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 132 IDLEGCIKTLRYFAGWADKI-QGRTIPTDD---NVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAE 207
Cdd:cd07099 77 LEVLLALEAIDWAARNAPRVlAPRKVPTGLlmpNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 208 QTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTvGAAISSHPhISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPC 287
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILD 367
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 368 LIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKN 447
Cdd:cd07099 314 HVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 448 LDKALKLASALESGTVWINC--YNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDvlLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
36-507 |
3.70e-122 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 367.72 E-value: 3.70e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 36 INNEWHESKsgKKFATYNPS-TLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAIL 114
Cdd:PRK03137 41 IGGERITTE--DKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFET---WKKWSPEDRARILLRAAAIIRRRKHEF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 115 ATLETMDTGKPFLHAFfIDLEGCIKTLRYFA----GWADKIQGRTIPTDDNvvcFTRHEPIGVCGAITPWNFPLLMLVWK 190
Cdd:PRK03137 116 SAWLVKEAGKPWAEAD-ADTAEAIDFLEYYArqmlKLADGKPVESRPGEHN---RYFYIPLGVGVVISPWNFPFAIMAGM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 191 LAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAAS 270
Cdd:PRK03137 192 TLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 271 RSN-----LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGD 345
Cdd:PRK03137 272 KVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGN 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 346 PFDiRTEQGPQIDQKQFDKILDLIESGKKEGaKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNI 425
Cdd:PRK03137 352 PED-NAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDF 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 426 EEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNAIYAQAPFGGFKMSGNGRELG--EYaLAEYTEVK 501
Cdd:PRK03137 430 DHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAIVGYHPFGGFNMSGTDSKAGgpDY-LLLFLQAK 508
|
....*.
gi 1952740663 502 TVTIKL 507
Cdd:PRK03137 509 TVSEMF 514
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
42-504 |
1.47e-121 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 366.51 E-value: 1.47e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 42 ESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAfQRGspWRRLDALGRGWLLHQLADLVERDRAILATLETMD 121
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA-QRA--WAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 122 TGKPFLHAF--FIDLEGCIktlRYFAGWADKI------QGrTIPTDDNVVcfTRHEPIGVCGAITPWNFPLLMLVWKLAP 193
Cdd:PRK09407 104 TGKARRHAFeeVLDVALTA---RYYARRAPKLlaprrrAG-ALPVLTKTT--ELRQPKGVVGVISPWNYPLTLAVSDAIP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 194 ALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISshPHISKIAFTGSTEVGKLVKEAASRsN 273
Cdd:PRK09407 178 ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGR-R 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 274 LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQ 353
Cdd:PRK09407 255 LIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 354 GPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRG-LFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRA 432
Cdd:PRK09407 335 GSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERA 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952740663 433 NSLEYGLTAAVFTKNLDKALKLASALESGTVWIN-CYNAIYA--QAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:PRK09407 415 NDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNeGYAAAWGsvDAPMGGMKDSGLGRRHGAEGLLKYTESQTIA 489
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
53-505 |
8.12e-118 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 354.36 E-value: 8.12e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 53 NPSTLEKICEVEEGDKLDVDKAVEAAhaafqrGSPWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFFi 132
Cdd:cd07146 5 NPYTGEVVGTVPAGTEEALREALALA------ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRY- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 133 DLEGCIKTLRYFAGWADKIQGRTIPTDDNV-----VCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAE 207
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGESFSCDLTAngkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 208 QTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASrsnLKRVTLELGGKNPC 287
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILD 367
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 368 LIESGKKEGAKLECGGsamEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKN 447
Cdd:cd07146 315 RVEEAIAQGARVLLGN---QRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952740663 448 LDKALKLASALESGTVWIN---CYNAiyAQAPFGGFKMSGNG-RELGEYALAEYTEVKTVTI 505
Cdd:cd07146 392 LDTIKRLVERLDVGTVNVNevpGFRS--ELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
54-504 |
5.10e-116 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 349.69 E-value: 5.10e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 54 PSTLEKICEVEEGDKLDVDKAVEAAHAAfQRGspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFfID 133
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA-QRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAF-EE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 134 LEGCIKTLRYFAGWADKI-----QGRTIPT-DDNVVCftrHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAE 207
Cdd:cd07101 79 VLDVAIVARYYARRAERLlkprrRRGAIPVlTRTTVN---RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 208 QTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHphISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPC 287
Cdd:cd07101 156 QTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGR-RLIGCSLELGGKNPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 288 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILD 367
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 368 LIESGKKEGAKLECGGSAMEDRG-LFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTK 446
Cdd:cd07101 313 HVDDAVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952740663 447 NLDKALKLASALESGTVWIN-CYNAIYA--QAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07101 393 DGARGRRIAARLRAGTVNVNeGYAAAWAsiDAPMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
32-504 |
2.83e-115 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 348.74 E-value: 2.83e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 32 TKIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDR 111
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA---WSATPVLKRQQVMFKFRQLLEENL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 112 AILATLETMDTGKPFLHAFFiDLEGCIKTLRYFAGWADKIQGRTIP-TDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWK 190
Cdd:cd07085 78 DELARLITLEHGKTLADARG-DVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 191 LAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGaAISSHPHISKIAFTGSTEVGKLVKEAAS 270
Cdd:cd07085 157 FPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVN-ALLDHPDIKAVSFVGSTPVGEYIYERAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 271 RSNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIR 350
Cdd:cd07085 236 ANG-KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 351 TEQGPQIDQKQFDKILDLIESGKKEGAKLECGG----SAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIE 426
Cdd:cd07085 315 ADMGPVISPAAKERIEGLIESGVEEGAKLVLDGrgvkVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 427 EVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINcynaIYAQAP-----FGGFKMS--GNGRELGEYALAEYTE 499
Cdd:cd07085 395 EAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN----VPIPVPlaffsFGGWKGSffGDLHFYGKDGVRFYTQ 470
|
....*
gi 1952740663 500 VKTVT 504
Cdd:cd07085 471 TKTVT 475
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
52-505 |
1.50e-112 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 340.76 E-value: 1.50e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 52 YNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQrgsPWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFF 131
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 132 iDLEGCIKTLRYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPA 206
Cdd:cd07147 81 -EVARAIDTFRIAAEEATRIYGEVLPLDisargEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 207 EQTPLTALYLGSLIKEVGFPPGVVNIVPGfgPTVGAAI-SSHPHISKIAFTGSTEVGKLVKEAASRsnlKRVTLELGGKN 285
Cdd:cd07147 160 SRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLlVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 286 PCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKI 365
Cdd:cd07147 235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 366 LDLIESGKKEGAKLECGGsamEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFT 445
Cdd:cd07147 315 EGWVNEAVDAGAKLLTGG---KRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952740663 446 KNLDKALKLASALESGTVWINCYNAIYA-QAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07147 392 RDLEKALRAWDELEVGGVVINDVPTFRVdHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
141-508 |
2.51e-112 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 338.63 E-value: 2.51e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 141 LRYFAGWADKIQGRTIPTD---DNVVCFTRhePIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLG 217
Cdd:PRK10090 41 IDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 218 SLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDL 297
Cdd:PRK10090 119 KIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 298 AVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRT-EQGPQIDQKQFDKILDLIESGKKEG 376
Cdd:PRK10090 198 AVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 377 AKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLAS 456
Cdd:PRK10090 278 ARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIK 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1952740663 457 ALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLD 508
Cdd:PRK10090 358 GLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQTQVVYLQSD 409
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
35-507 |
3.73e-111 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 338.42 E-value: 3.73e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 35 FINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFqrgSPWRRLDALGRGWLLHQLADLVERDRAIL 114
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL---PAWRALTAKERANILRRWFNLMMEHQDDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 115 ATLETMDTGKPFLHAffidlEGCIKT----LRYFAGWADKIQGRTIP---TDDNVVCFTrhEPIGVCGAITPWNFPLLML 187
Cdd:PRK11241 91 ARLMTLEQGKPLAEA-----KGEISYaasfIEWFAEEGKRIYGDTIPghqADKRLIVIK--QPIGVTAAITPWNFPAAMI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 188 VWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKE 267
Cdd:PRK11241 164 TRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLME 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 268 AASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPF 347
Cdd:PRK11241 244 QCAK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 348 DIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEE 427
Cdd:PRK11241 323 EKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEAD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 428 VIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 507
Cdd:PRK11241 403 VIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
34-504 |
1.79e-110 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 337.61 E-value: 1.79e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 34 IFINNEWHESKSgkKFATYNPS-TLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRA 112
Cdd:TIGR01237 35 LVINGERVETEN--KIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEA---WKKTDPEERAAILFKAAAIVRRRRH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 113 ILATLETMDTGKPFLHAFfIDLEGCIKTLRYFAGWADKIQGR----TIPTDDNVVCFTrhePIGVCGAITPWNFPLLMLV 188
Cdd:TIGR01237 110 EFSALLVKEVGKPWNEAD-AEVAEAIDFMEYYARQMIELAKGkpvnSREGETNQYVYT---PTGVTVVISPWNFPFAIMV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 189 WKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEA 268
Cdd:TIGR01237 186 GMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFER 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 269 ASR-----SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPI 343
Cdd:TIGR01237 266 AAKvqpgqKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 344 GDPFDIRTEQGPQIDQKQFDKILDLIESGKKEGaKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFK 423
Cdd:TIGR01237 346 GPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRAS 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 424 NIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNAIYAQAPFGGFKMSGNGRELG--EYaLAEYTE 499
Cdd:TIGR01237 425 DFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNrnITGAIVGYQPFGGFKMSGTDSKAGgpDY-LALFMQ 503
|
....*
gi 1952740663 500 VKTVT 504
Cdd:TIGR01237 504 AKTVT 508
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
52-504 |
1.28e-105 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 323.48 E-value: 1.28e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 52 YNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFF 131
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQRE---WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 132 idleGCIKTLryfagwADKIQ-----G----RTIPTDDNVVCFTR-----HEPIGVCGAITPWNFPLLMLVWKLAPALCC 197
Cdd:cd07098 78 ----GEILVT------CEKIRwtlkhGekalRPESRPGGLLMFYKrarveYEPLGVVGAIVSWNYPFHNLLGPIIAALFA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 198 GNTIVVKPAEQTPLTALYLGSLIKEV----GFPPGVVNIVPGFGPTvGAAISSHPHISKIAFTGSTEVGKLVKEAASRSn 273
Cdd:cd07098 148 GNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 274 LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQ 353
Cdd:cd07098 226 LTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 354 GPQIDQKQFDKILDLIESGKKEGAKLECGGS----AMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVI 429
Cdd:cd07098 306 GAMISPARFDRLEELVADAVEKGARLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAV 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952740663 430 KRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIY--AQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:cd07098 386 EIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYyvQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
45-503 |
3.35e-105 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 322.87 E-value: 3.35e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 45 SGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgSPWRRLDALgRGWLLHQLADLVERDRAILATLETMDTGK 124
Cdd:TIGR04284 13 SAGTFPTVNPATEEVLGVAADATAADMDAAIAAARRAFDE-TDWSRDTAL-RVRCLRQLRDALRAHVEELRELTIAEVGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 125 PFLHAFFIDLEGCIKTLRYFAGWADKIQGRT---------IPTDDNVvcftRHEPIGVCGAITPWNFPLLMLVWKLAPAL 195
Cdd:TIGR04284 91 PRMLTAGAQLEGPVDDLGFAADLAESYAWTTdlgvaspmgIPTRRTL----RREAVGVVGAITPWNFPHQINLAKLGPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 196 CCGNTIVVKPAEQTPLTALYLGSLIKE-VGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRSnL 274
Cdd:TIGR04284 167 AAGNTVVLKPAPDTPWCAAVLGELIAEhTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRAVMADAAAT-L 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 275 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQG 354
Cdd:TIGR04284 246 KKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGDPADPGTVCG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 355 PQIDQKQFDKILDLIESGKKEGAKLECGGS--AMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRA 432
Cdd:TIGR04284 326 PVISARQRDRVQSYLDLAVAEGGRFACGGGrpADRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDDDAVRIA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952740663 433 NSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:TIGR04284 406 NDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETKLI 476
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
52-503 |
4.23e-103 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 316.50 E-value: 4.23e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 52 YNPSTLEKICEVEEGDKLDVDKAVEAAHAAfQRGspWRRLDALGRGWLLHQ-LADLVERDRAILATLETMdTGKPFLHAf 130
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAA-QKG--WRAVPLEERKAIVTRaVELLAANTDEIAEELTWQ-MGRPIAQA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 131 fidlEGCIKTL----RYFAGWADK-IQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKP 205
Cdd:cd07102 76 ----GGEIRGMleraRYMISIAEEaLADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 206 AEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTvGAAISSHPHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKN 285
Cdd:cd07102 152 SPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 286 PCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKI 365
Cdd:cd07102 230 PAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 366 LDLIESGKKEGAKLECGG---SAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAA 442
Cdd:cd07102 310 RAQIADAIAKGARALIDGalfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTAS 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952740663 443 VFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07102 390 VWTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
22-504 |
2.21e-95 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 298.34 E-value: 2.21e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 22 RPVRSLEVEFTKIFINNEWHESKSGKkfATYNPS-TLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLL 100
Cdd:cd07083 9 RRVKEEFGRAYPLVIGGEWVDTKERM--VSVSPFaPSEVVGTTAKADKAEAEAALEAAWAAFKT---WKDWPQEDRARLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 101 HQLADLVERDRAILATLETMDTGKPFLHAFfIDLEGCIKTLRYFAGWADKIQGR-----TIPTDDNVvcfTRHEPIGVCG 175
Cdd:cd07083 84 LKAADLLRRRRRELIATLTYEVGKNWVEAI-DDVAEAIDFIRYYARAALRLRYPavevvPYPGEDNE---SFYVGLGAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 176 AITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAF 255
Cdd:cd07083 160 VISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 256 TGSTEVGKLVKEAASR-----SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEF 330
Cdd:cd07083 240 TGSLETGKKIYEAAARlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 331 VRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIESGKKEGaKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKE 410
Cdd:cd07083 320 LERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 411 EIFGPVQPILKFKNIE--EVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNAIYAQAPFGGFKMSG-N 485
Cdd:cd07083 399 EIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkITGALVGVQPFGGFKLSGtN 478
|
490
....*....|....*....
gi 1952740663 486 GRELGEYALAEYTEVKTVT 504
Cdd:cd07083 479 AKTGGPHYLRRFLEMKAVA 497
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
37-505 |
2.14e-94 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 294.88 E-value: 2.14e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 37 NNEWheSKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAILAT 116
Cdd:cd07130 4 DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE---WRDVPAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 117 LETMDTGKPFLHAF-----FIDLegCiktlRYFAGWADKIQGRTIPTD--DNVVCFTRHePIGVCGAITPWNFPLLMLVW 189
Cdd:cd07130 79 LVSLEMGKILPEGLgevqeMIDI--C----DFAVGLSRQLYGLTIPSErpGHRMMEQWN-PLGVVGVITAFNFPVAVWGW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 190 KLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEV----GFPPGVVNIVPGfGPTVGAAISSHPHISKIAFTGSTEVGKLV 265
Cdd:cd07130 152 NAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 266 KEAASRsNLKRVTLELGGKNPCIVCADADLDLAVecahQGVFF----NQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKR 341
Cdd:cd07130 231 GQAVAA-RFGRSLLELGGNNAIIVMEDADLDLAV----RAVLFaavgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 342 PIGDPFDIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFsEVTDTMRIAKEEIFGPVQPILK 421
Cdd:cd07130 306 RIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIV-EGLSDAPIVKEETFAPILYVLK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 422 FKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCyNAIYAQA----PFGGFKMSGNGRELGEYALAEY 497
Cdd:cd07130 385 FDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSDCGIVNV-NIGTSGAeiggAFGGEKETGGGRESGSDAWKQY 463
|
....*...
gi 1952740663 498 TEVKTVTI 505
Cdd:cd07130 464 MRRSTCTI 471
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
50-505 |
3.43e-92 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 288.56 E-value: 3.43e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 50 ATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPfLHA 129
Cdd:PRK09406 4 ATINPATGETVKTFTALTDDEVDAAIARAHARFRD---YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT-LAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 130 FFIDLEGCIKTLRYFAGWADKIQGRTiPTDDNVV----CFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKP 205
Cdd:PRK09406 80 AKAEALKCAKGFRYYAEHAEALLADE-PADAAAVgasrAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 206 AEQTPLTALYLGSLIKEVGFPPGVVNIVpgfgpTVGA----AISSHPHISKIAFTGSTEVGKLVKEAASRSnLKRVTLEL 281
Cdd:PRK09406 159 ASNVPQTALYLADLFRRAGFPDGCFQTL-----LVGSgaveAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVLEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 282 GGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQ 361
Cdd:PRK09406 233 GGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 362 FDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTA 441
Cdd:PRK09406 313 RDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952740663 442 AVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:PRK09406 393 NAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
35-505 |
2.04e-84 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 270.22 E-value: 2.04e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 35 FINNEWHESKSGKkfATYNPSTLEK-ICEVEEGDKLDVDKAVEAAHAAFqrgSPWRRLDALGRGWLLHQLADLVERDRAI 113
Cdd:cd07125 36 IINGEETETGEGA--PVIDPADHERtIGEVSLADAEDVDAALAIAAAAF---AGWSATPVEERAEILEKAADLLEANRGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 114 LATLETMDTGKPFLHAF-----FIDLegciktLRYFAGWADKIQGRTI---PTD--DNVVCftrhEPIGVCGAITPWNFP 183
Cdd:cd07125 111 LIALAAAEAGKTLADADaevreAIDF------CRYYAAQARELFSDPElpgPTGelNGLEL----HGRGVFVCISPWNFP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 184 LLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGK 263
Cdd:cd07125 181 LAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 264 LVKEAASRSNLKRVTL--ELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKR 341
Cdd:cd07125 261 LINRALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 342 PIGDPFDIRTEQGPQIDQKQFDKILDLIESGKKEgAKLECGGSAMEDRGLFIKPTVFSEV-TDTMRiakEEIFGPVQPIL 420
Cdd:cd07125 341 KVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVgIFDLT---TEVFGPILHVI 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 421 KFK--NIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINcYN---AIYAQAPFGGFKMSGNGRELG--EYa 493
Cdd:cd07125 417 RFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN-RNitgAIVGRQPFGGWGLSGTGPKAGgpNY- 494
|
490
....*....|..
gi 1952740663 494 LAEYTEVKTVTI 505
Cdd:cd07125 495 LLRFGNEKTVSL 506
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
53-505 |
1.39e-82 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 263.51 E-value: 1.39e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 53 NPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRGSPWrrLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFF- 131
Cdd:cd07148 5 NPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 132 ----ID-LEGCIKTLRYFAGwadkiqgRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTI 201
Cdd:cd07148 83 vtraIDgVELAADELGQLGG-------REIPMGltpasAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 202 VVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGfGPTVGAAISSHPHISKIAFTGSTEVGKLVkeaasRSNLK---RVT 278
Cdd:cd07148 156 IVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPC-ENAVAEKLVTDPRVAFFSFIGSARVGWML-----RSKLApgtRCA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 279 LELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQID 358
Cdd:cd07148 230 LEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 359 QKQFDKILDLIESGKKEGAKLECGGSAMEDRGLfiKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYG 438
Cdd:cd07148 310 PREVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952740663 439 LTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQ-APFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07148 388 FQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI 455
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
74-505 |
5.24e-80 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 255.91 E-value: 5.24e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 74 AVEAAHAAFQRGS----PWRR--LDALGRGwllhqladLVERDRAILATLETmDTGKPFLHAFFIDLEGCIK----TLRY 143
Cdd:cd07087 3 LVARLRETFLTGKtrslEWRKaqLKALKRM--------LTENEEEIAAALYA-DLGKPPAEAYLTEIAVVLGeidhALKH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 144 FAGWADKiqgRTIPTDDNVV---CFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLI 220
Cdd:cd07087 74 LKKWMKP---RRVSVPLLLQpakAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 221 KEVgFPPGVVNIVPGfGPTVGAAISSHP--HIskiAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLA 298
Cdd:cd07087 151 PKY-FDPEAVAVVEG-GVEVATALLAEPfdHI---FFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 299 VECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEyAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIESGKkegak 378
Cdd:cd07087 225 ARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKK-AIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGK----- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 379 LECGGSAMEDRgLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASAL 458
Cdd:cd07087 299 VVIGGQVDKEE-RYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAET 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1952740663 459 ESGTVwinCYNAIYAQA-----PFGGFKMSGNGRELGEYALAEYTEVKTVTI 505
Cdd:cd07087 378 SSGGV---CVNDVLLHAaipnlPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
53-503 |
6.26e-78 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 251.70 E-value: 6.26e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 53 NPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVeRDRAI-LATLETMDTGKPFLHAff 131
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRD---WRETNIDYRAQKLRDIGKAL-RARSEeMAQMITREMGKPINQA-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 132 idlEGCIKTLRYFAGWADKiQG----RTIPT-DDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPA 206
Cdd:PRK13968 87 ---RAEVAKSANLCDWYAE-HGpamlKAEPTlVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 207 EQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISShPHISKIAFTGSTEVGKLVKEAASRSnLKRVTLELGGKNP 286
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 287 CIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKIL 366
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 367 DLIESGKKEGAKLECGGSAMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTK 446
Cdd:PRK13968 321 HQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTT 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952740663 447 NLDKALKLASALESGTVWINCYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:PRK13968 401 DETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
70-498 |
1.05e-77 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 250.27 E-value: 1.05e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 70 DVDKAVEAAHAAFqrgSPWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFF--------IDLEgcIKTL 141
Cdd:cd07095 1 QVDAAVAAARAAF---PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTevaamagkIDIS--IKAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 142 RYFAGwadkiqGRTIPTDdNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIK 221
Cdd:cd07095 76 HERTG------ERATPMA-QGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 222 EVGFPPGVVNIVPGfGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVEC 301
Cdd:cd07095 149 EAGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 302 AHQGVFFNQGQCCTAASRVFVEE-QIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIESGKKEGAKLE 380
Cdd:cd07095 228 IVQSAFLTAGQRCTCARRLIVPDgAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 381 CGGSAMEDRGLFIKPTVFsEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALES 460
Cdd:cd07095 308 LAMERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRA 386
|
410 420 430
....*....|....*....|....*....|....*....
gi 1952740663 461 GTV-WINCYNAIYAQAPFGGFKMSGNGRELGEYAlAEYT 498
Cdd:cd07095 387 GIVnWNRPTTGASSTAPFGGVGLSGNHRPSAYYA-ADYC 424
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
33-511 |
2.08e-77 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 251.21 E-value: 2.08e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 33 KIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAfQRGspWRRLDALGRGWLLHQLADLVERDRA 112
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA-QKA--WAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 113 ILATLETMDTGKPFLHAF--------FIDL---EGCiktlRYFAgwadkiQGRTIPTDD------NVVCFTRHEPIGVCG 175
Cdd:PLN00412 94 PIAECLVKEIAKPAKDAVtevvrsgdLISYtaeEGV----RILG------EGKFLVSDSfpgnerNKYCLTSKIPLGVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 176 AITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAF 255
Cdd:PLN00412 164 AIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 256 TGStEVGKLVKEAASRSNLKrvtLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSV 335
Cdd:PLN00412 244 TGG-DTGIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 336 EYAKKRPIGDPFDiRTEQGPQIDQKQFDKILDLIESGKKEGAKLeCGGSAMEdrGLFIKPTVFSEVTDTMRIAKEEIFGP 415
Cdd:PLN00412 320 AKVAKLTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATF-CQEWKRE--GNLIWPLLLDNVRPDMRIAWEEPFGP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 416 VQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYA-QAPFGGFKMSGNGRELGEYAL 494
Cdd:PLN00412 396 VLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIGSQGITNSI 475
|
490
....*....|....*..
gi 1952740663 495 AEYTEVKTVTIKLDDKS 511
Cdd:PLN00412 476 NMMTKVKSTVINLPKPS 492
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
164-503 |
1.12e-76 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 247.52 E-value: 1.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 164 CFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGfGPTVGAA 243
Cdd:cd07134 94 SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-DAEVAQA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 244 ISSHP--HIskiAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVF 321
Cdd:cd07134 172 LLELPfdHI---FFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVF 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 322 VEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQI-DQKQFDKILDLIESGKKEGAKLECGGsAMEDRGLFIKPTVFSE 400
Cdd:cd07134 248 VHESVKDAFVEHLKAEIEKFYGKDAARKASPDLARIvNDRHFDRLKGLLDDAVAKGAKVEFGG-QFDAAQRYIAPTVLTN 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 401 VTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVwinCYNAIYAQA----- 475
Cdd:cd07134 327 VTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGV---VVNDVVLHFlnpnl 403
|
330 340
....*....|....*....|....*...
gi 1952740663 476 PFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07134 404 PFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
169-492 |
8.47e-72 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 235.09 E-value: 8.47e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 169 EPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGfGPTVGAAISSHP 248
Cdd:cd07136 99 EPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEENQELLDQK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 249 hISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYP 328
Cdd:cd07136 177 -FDYIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 329 EFVRRSVEYAKKRPIGDPFDirTEQGPQI-DQKQFDKILDLIESGKkegakLECGGSAmEDRGLFIKPTVFSEVTDTMRI 407
Cdd:cd07136 255 KFIKELKEEIKKFYGEDPLE--SPDYGRIiNEKHFDRLAGLLDNGK-----IVFGGNT-DRETLYIEPTILDNVTWDDPV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 408 AKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINcyNAIYAQA----PFGGFKMS 483
Cdd:cd07136 327 MQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN--DTIMHLAnpylPFGGVGNS 404
|
....*....
gi 1952740663 484 GNGRELGEY 492
Cdd:cd07136 405 GMGSYHGKY 413
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
70-503 |
3.60e-70 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 230.57 E-value: 3.60e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 70 DVDKAVEAAHAAFQRGS----PWRRldalgrgWLLHQLADLVERDRAILATLETMDTGKPFLHAFFIDLEGC-------I 138
Cdd:cd07135 6 EIDSIHSRLRATFRSGKtkdlEYRL-------WQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVkndilhmL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 139 KTLRYFAgwADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGS 218
Cdd:cd07135 79 KNLKKWA--KDEKVKDGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 219 LIKEvGFPPGVVNIVPGFGPTVGAAISShpHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLA 298
Cdd:cd07135 157 LVPK-YLDPDAFQVVQGGVPETTALLEQ--KFDKIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLELA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 299 VECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDiRTEQGPQIDQKQFDKILDLIESGKkegAK 378
Cdd:cd07135 233 AKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANA-SPDYTRIVNPRHFNRLKSLLDTTK---GK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 379 LECGGSaMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKnlDKALK---LA 455
Cdd:cd07135 309 VVIGGE-MDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTD--DKSEIdhiLT 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1952740663 456 SALESGTVWINCY-NAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07135 386 RTRSGGVVINDTLiHVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
33-504 |
3.78e-69 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 229.38 E-value: 3.78e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 33 KIFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFqrgSPWRRLDALGRGWLLHQLADLVERDRA 112
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF---LTWGQTSLAQRTSVLLRYQALLKEHRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 113 ILATLETMDTGKPFLHAFFiDLEGCIKTLRYFAGWADKIQGRTIPT-DDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKL 191
Cdd:TIGR01722 79 EIAELITAEHGKTHSDALG-DVARGLEVVEHACGVNSLLKGETSTQvATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 192 APALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGaAISSHPHISKIAFTGSTEVGKLVKEAASR 271
Cdd:TIGR01722 158 PIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVD-RLLEHPDVKAVSFVGSTPIGRYIHTTGSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 272 SNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIyPEFVRRSVEYAKKRPIGDPFDIRT 351
Cdd:TIGR01722 237 HG-KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 352 EQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAME----DRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEE 427
Cdd:TIGR01722 315 EMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKvdgyEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 428 VIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCynAIYAQAP---FGGFKMS--GNGRELGEYALAEYTEVKT 502
Cdd:TIGR01722 395 AIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNV--PIPVPLPyfsFTGWKDSffGDHHIYGKQGTHFYTRGKT 472
|
..
gi 1952740663 503 VT 504
Cdd:TIGR01722 473 VT 474
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
167-503 |
6.94e-68 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 224.67 E-value: 6.94e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 167 RHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGfGPTVGAAISS 246
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTG-GADVAAAFSS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 247 HP--HIskiAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEE 324
Cdd:cd07133 176 LPfdHL---LFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 325 QIYPEFVRRSVEYAKKR-PigdpfDIRTeqGPQ----IDQKQFDKILDLIESGKKEGAKL-ECGGSAMEDRGL-FIKPTV 397
Cdd:cd07133 252 DKLEEFVAAAKAAVAKMyP-----TLAD--NPDytsiINERHYARLQGLLEDARAKGARViELNPAGEDFAATrKLPPTL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 398 FSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINcyNAIY--AQ- 474
Cdd:cd07133 325 VLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIN--DTLLhvAQd 402
|
330 340 350
....*....|....*....|....*....|
gi 1952740663 475 -APFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07133 403 dLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
11-484 |
2.06e-67 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 225.93 E-value: 2.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 11 GQPDRKppALPRPVRSLEVEFTKI--FINNEwhESKSGKKFATYNPST-LEKICEVEEGDKLDVDKAVEAAHAAfqRGSp 87
Cdd:cd07123 12 GSPERA--KLQEALAELKSLTVEIplVIGGK--EVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEA--RKE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 88 WRRLDALGRGWLLHQLADLVE---RDRAILATLetMDTGKPFLHAFfIDlEGC--IKTLRYFAGWADKI-QGRTIPTDDN 161
Cdd:cd07123 85 WARMPFEDRAAIFLKAADLLSgkyRYELNAATM--LGQGKNVWQAE-ID-AACelIDFLRFNVKYAEELyAQQPLSSPAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 162 VVCFTRHEPI-GVCGAITPWNFPLLMLVWKLAPALCcGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTV 240
Cdd:cd07123 161 VWNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 241 GAAISSHPHISKIAFTGSTEVGK-LVKEAASR----SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCT 315
Cdd:cd07123 240 GDTVLASPHLAGLHFTGSTPTFKsLWKQIGENldryRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 316 AASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIESGKKE-GAKLECGGSAMEDRGLFIK 394
Cdd:cd07123 320 AASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 395 PTVFsEVTDTM-RIAKEEIFGPVQPILKF--KNIEEVIKRANSL-EYGLTAAVFTKNlDKALKLAS-ALE--SGTVWIN- 466
Cdd:cd07123 400 PTVI-ETTDPKhKLMTEEIFGPVLTVYVYpdSDFEETLELVDTTsPYALTGAIFAQD-RKAIREATdALRnaAGNFYINd 477
|
490
....*....|....*....
gi 1952740663 467 -CYNAIYAQAPFGGFKMSG 484
Cdd:cd07123 478 kPTGAVVGQQPFGGARASG 496
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
62-505 |
2.40e-67 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 234.32 E-value: 2.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 62 EVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKpflhaffiDLEGCIKT- 140
Cdd:PRK11904 578 EVAFADAEQVEQALAAARAAFPA---WSRTPVEERAAILERAADLLEANRAELIALCVREAGK--------TLQDAIAEv 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 141 ------LRYFAGWADKIQGRTI----PT-DDNVVcftRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQT 209
Cdd:PRK11904 647 reavdfCRYYAAQARRLFGAPEklpgPTgESNEL---RLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQT 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 210 PLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEA-ASRSNlKRVTL--ELGGKNP 286
Cdd:PRK11904 724 PLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTlAARDG-PIVPLiaETGGQNA 802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 287 CIVCADADLDLAVECAHQGVFFNQGQCCTAAsRV-FVEEQIYP---EFVRRSVEYAKkrpIGDPFDIRTEQGPQIDQKQF 362
Cdd:PRK11904 803 MIVDSTALPEQVVDDVVTSAFRSAGQRCSAL-RVlFVQEDIADrviEMLKGAMAELK---VGDPRLLSTDVGPVIDAEAK 878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 363 DKILDLIESGKKEG---AKLECGGSAmeDRGLFIKPTVFsEVtDTMRIAKEEIFGPVQPILKFK--NIEEVIKRANSLEY 437
Cdd:PRK11904 879 ANLDAHIERMKREArllAQLPLPAGT--ENGHFVAPTAF-EI-DSISQLEREVFGPILHVIRYKasDLDKVIDAINATGY 954
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952740663 438 GLTAAVFTKNLDKALKLASALESGTVWINcYNAIYA----QaPFGGFKMSGNG-RELGEYALAEYTEVKTVTI 505
Cdd:PRK11904 955 GLTLGIHSRIEETADRIADRVRVGNVYVN-RNQIGAvvgvQ-PFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1025
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
42-486 |
4.42e-67 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 234.45 E-value: 4.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 42 ESKSGKKFATYNPSTLEKIC-EVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADLVERDRAILATLETM 120
Cdd:COG4230 565 EAASGEARPVRNPADHSDVVgTVVEATAADVEAALAAAQAAFPA---WSATPVEERAAILERAADLLEAHRAELMALLVR 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 121 DTGKPFLHA---------FfidlegciktLRYFAGwadkiQGRTIPTDDnvvcfTRHEPIGVCGAITPWNFPLLMLVWKL 191
Cdd:COG4230 642 EAGKTLPDAiaevreavdF----------CRYYAA-----QARRLFAAP-----TVLRGRGVFVCISPWNFPLAIFTGQV 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 192 APALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVkeaaSR 271
Cdd:COG4230 702 AAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLI----NR 777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 272 SNLKR----VTL--ELGGKNPCIV---------CADadldlAVECAhqgvFFNQGQCCTAAsRV-FVEEQIYPEFVRRSV 335
Cdd:COG4230 778 TLAARdgpiVPLiaETGGQNAMIVdssalpeqvVDD-----VLASA----FDSAGQRCSAL-RVlCVQEDIADRVLEMLK 847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 336 EYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIESGKKEGAKL-ECGGSAMEDRGLFIKPTVFsEVtDTMRIAKEEIFG 414
Cdd:COG4230 848 GAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVAPTLI-EI-DSISDLEREVFG 925
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952740663 415 PVQPILKFK--NIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINcYNAIYA----QaPFGGFKMSGNG 486
Cdd:COG4230 926 PVLHVVRYKadELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN-RNIIGAvvgvQ-PFGGEGLSGTG 1001
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
35-512 |
7.82e-65 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 218.55 E-value: 7.82e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 35 FINNEWheSKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAfqrGSPWRRLDALGRGWLLHQLADLVERDRAIL 114
Cdd:PLN02315 24 YVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEA---AKIWMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 115 ATLETMDTGKpFLHAFFIDLEGCIKTLRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAP 193
Cdd:PLN02315 99 GRLVSLEMGK-ILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 194 ALCCGNTIVVKPAEQTPLTALYLGSLIKEV----GFPPGVVNIVPGfGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAA 269
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 270 SrSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDI 349
Cdd:PLN02315 257 N-ARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 350 RTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAMEDRGLFIKPTVFsEVTDTMRIAKEEIFGPVQPILKFKNIEEVI 429
Cdd:PLN02315 336 GTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAI 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 430 KRANSLEYGLTAAVFTKNLDKALKLASALES--GTVWINC-YNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:PLN02315 415 EINNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTIN 494
|
....*.
gi 1952740663 507 LDDKSP 512
Cdd:PLN02315 495 YGNELP 500
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
35-497 |
1.43e-64 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 217.52 E-value: 1.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 35 FINNEWHESkSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFqrgSPWRRLDALGRGWLLHQLADLVERDRAIL 114
Cdd:PRK09457 4 WINGDWIAG-QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF---PAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 115 ATLETMDTGKPFLHAffidlegciKTlrYFAGWADKI-------QGRT----IPTDDNVVCFtRHEPIGVCGAITPWNFP 183
Cdd:PRK09457 80 AEVIARETGKPLWEA---------AT--EVTAMINKIaisiqayHERTgekrSEMADGAAVL-RHRPHGVVAVFGPYNFP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 184 LLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGfGPTVGAAISSHPHISKIAFTGSTEVGK 263
Cdd:PRK09457 148 GHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 264 LV-KEAASRSNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPE-FVRRSVEYAKKR 341
Cdd:PRK09457 227 LLhRQFAGQPE-KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 342 PIGDPFDirTEQ---GPQIDQKQFDKILD----LIESGKK---EGAKLECGGSamedrglFIKPTVFsEVTDTMRIAKEE 411
Cdd:PRK09457 306 TVGRWDA--EPQpfmGAVISEQAAQGLVAaqaqLLALGGKsllEMTQLQAGTG-------LLTPGII-DVTGVAELPDEE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 412 IFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTV-WINCYNAIYAQAPFGGFKMSGNGRELG 490
Cdd:PRK09457 376 YFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNHRPSA 455
|
....*..
gi 1952740663 491 EYAlAEY 497
Cdd:PRK09457 456 YYA-ADY 461
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
60-490 |
1.62e-64 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 217.47 E-value: 1.62e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 60 ICEVEEGDKLDVDKAVEAAHAAFqrgSPWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFlHAFFIDLEGCIK 139
Cdd:TIGR01238 65 VGQVFHANLAHVQAAIDSAQQAF---PTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTI-HNAIAEVREAVD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 140 TLRYFAGWADKiqgrTIPTDDnvvcftrHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSL 219
Cdd:TIGR01238 141 FCRYYAKQVRD----VLGEFS-------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVEL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 220 IKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLVKEAASRSNLKRVTL--ELGGKNPCIVCADADLDL 297
Cdd:TIGR01238 210 MQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIVDSTALPEQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 298 AVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIESGKKEG- 376
Cdd:TIGR01238 290 VVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQk 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 377 --AKLECGGSAMEDRGLFIKPTVFSevTDTMRIAKEEIFGPVQPILKFK--NIEEVIKRANSLEYGLTAAVFTKNLDKAL 452
Cdd:TIGR01238 370 kiAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTMGVHSRIETTYR 447
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1952740663 453 KLASALESGTVWIN--CYNAIYAQAPFGGFKMSGNGRELG 490
Cdd:TIGR01238 448 WIEKHARVGNCYVNrnQVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
35-486 |
5.16e-64 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 225.51 E-value: 5.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 35 FINNEWH-------ESKSGKKFATYNPS-TLEKICEVEEGDKLDVDKAVEAAHAAFQRgspWRRLDALGRGWLLHQLADL 106
Cdd:PRK11905 548 FAAKTWHaapllagGDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPE---WSATPAAERAAILERAADL 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 107 VERDRAILATLETMDTGKPFLHAffID-LEGCIKTLRYFAGwadkiQGRTIPTDDnvvcftRHEPIGVCGAITPWNFPLL 185
Cdd:PRK11905 625 MEAHMPELFALAVREAGKTLANA--IAeVREAVDFLRYYAA-----QARRLLNGP------GHKPLGPVVCISPWNFPLA 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 186 MLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLV 265
Cdd:PRK11905 692 IFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLI 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 266 -KEAASRSNlKRVTL--ELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAAsRV-FVEEQIYPEFVRRSVEYAKKR 341
Cdd:PRK11905 772 qRTLAKRSG-PPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSAL-RVlCLQEDVADRVLTMLKGAMDEL 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 342 PIGDPFDIRTEQGPQIDQKQFDKILDLIESGKKEGAKL-ECGGSAMEDRGLFIKPTVFsEVTDtMRIAKEEIFGPVQPIL 420
Cdd:PRK11905 850 RIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLI-EIDS-ISDLEREVFGPVLHVV 927
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952740663 421 KFK--NIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINcYNAIYA----QaPFGGFKMSGNG 486
Cdd:PRK11905 928 RFKadELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN-RNIIGAvvgvQ-PFGGEGLSGTG 997
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
164-506 |
1.45e-61 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 209.50 E-value: 1.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 164 CFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGfGPTVGAA 243
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 244 ISSHPhISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVE 323
Cdd:PTZ00381 181 LLKEP-FDHIFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 324 EQIYPEFVrRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIESgkkEGAKLECGGSA-MEDRglFIKPTVFSEVT 402
Cdd:PTZ00381 259 RSIKDKFI-EALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGEVdIENK--YVAPTIIVNPD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 403 DTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNAIYAQAPFGGF 480
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFGGV 412
|
330 340
....*....|....*....|....*.
gi 1952740663 481 KMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:PTZ00381 413 GNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
9-509 |
5.19e-58 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 202.67 E-value: 5.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 9 ENGQPdRKPPALPRpvrsleveftkiFINNEWHESKSGKKFATYNPSTLEKICEVEEGDKLDVDKAVEAAHAAFQRgspW 88
Cdd:PLN02419 104 QSTQP-QMPPRVPN------------LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL---W 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 89 RRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPfLHAFFIDLEGCIKTLRYFAGWADKIQGRTIPTDDNVV-CFTR 167
Cdd:PLN02419 168 RNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKT-LKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVdTYSI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 168 HEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGaAISSH 247
Cdd:PLN02419 247 REPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDD 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 248 PHISKIAFTGSTEVG-KLVKEAASRSnlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASR-VFVEEQ 325
Cdd:PLN02419 326 EDIRAVSFVGSNTAGmHIYARAAAKG--KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 326 iyPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAM----EDRGLFIKPTVFSEV 401
Cdd:PLN02419 404 --KSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpgYEKGNFIGPTILSGV 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 402 TDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCynAIYAQAPFggFK 481
Cdd:PLN02419 482 TPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPF--FS 557
|
490 500 510
....*....|....*....|....*....|....*
gi 1952740663 482 MSGNGREL-------GEYALAEYTEVKTVTIKLDD 509
Cdd:PLN02419 558 FTGNKASFagdlnfyGKAGVDFFTQIKLVTQKQKD 592
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
73-506 |
2.38e-56 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 194.36 E-value: 2.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 73 KAVEAAHAAFQRGSPwRRLDalgrgWLLHQLADLV----ERDRAILATLEtMDTGKPFLHAFFIDLEGCIKTLRY----F 144
Cdd:cd07132 2 EAVRRAREAFSSGKT-RPLE-----FRIQQLEALLrmleENEDEIVEALA-KDLRKPKFEAVLSEILLVKNEIKYaisnL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 145 AGWA-DKIQGRTIPT--DDnvvCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLI- 220
Cdd:cd07132 75 PEWMkPEPVKKNLATllDD---VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIp 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 221 ----KEVgFPpgVVNivpgfgptvgAAISSHPHISK-----IAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCA 291
Cdd:cd07132 152 kyldKEC-YP--VVL----------GGVEETTELLKqrfdyIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 292 DADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVrrsvEYAK---KRPIGDpfDIRTEQ--GPQIDQKQFDKIL 366
Cdd:cd07132 218 SCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFV----EALKktlKEFYGE--DPKESPdyGRIINDRHFQRLK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 367 DLIESGKkegakLECGGSaMEDRGLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTK 446
Cdd:cd07132 292 KLLSGGK-----VAIGGQ-TDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSN 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952740663 447 NLDKALKLASALESGTVwinCYN-----AIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 506
Cdd:cd07132 366 NKKVINKILSNTSSGGV---CVNdtimhYTLDSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
70-503 |
1.42e-51 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 181.46 E-value: 1.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 70 DVDKAVEAAHAAFQRGSPWRrLDALGRGWLLhqladLVERDRAILATLETmDTGKPFLHAFFIDL----EGCIKTLRYFA 145
Cdd:cd07137 4 LVRELRETFRSGRTRSAEWR-KSQLKGLLRL-----VDENEDDIFAALRQ-DLGKPSAESFRDEVsvlvSSCKLAIKELK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 146 GWAD----KIQGRTIPTDDNVVCftrhEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIK 221
Cdd:cd07137 77 KWMApekvKTPLTTFPAKAEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 222 EVgFPPGVVNIVPGfGPTVGAAISSHpHISKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVEC 301
Cdd:cd07137 153 EY-LDTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAVRR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 302 AHQGVF-FNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPfdIRTEQGPQIDQKQFDKILDLIESGKKEGAKLE 380
Cdd:cd07137 229 IAGGKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENP--KESKDLSRIVNSHHFQRLSRLLDDPSVADKIV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 381 CGGSAMEDRgLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALES 460
Cdd:cd07137 307 HGGERDEKN-LYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSS 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1952740663 461 GTVWINCYNAIYA--QAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:cd07137 386 GGVTFNDTVVQYAidTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
53-486 |
6.36e-46 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 172.85 E-value: 6.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 53 NPSTLEKIC-EVEEGDKLDVDKAVEAAHAAfqrGSPWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFf 131
Cdd:PRK11809 665 NPADPRDIVgYVREATPAEVEQALESAVNA---APIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAI- 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 132 IDLEGCIKTLRYFAGwadkiQGRTIPTDDNvvcftrHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPL 211
Cdd:PRK11809 741 AEVREAVDFLRYYAG-----QVRDDFDNDT------HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPL 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 212 TALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGKLV-KEAASR-SNLKRVT---LELGGKNP 286
Cdd:PRK11809 810 IAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLqRNLAGRlDPQGRPIpliAETGGQNA 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 287 CIVCADADLDLAVECAHQGVFFNQGQCCTA----------ASRVFveeqiypEFVRRSV-EYAkkrpIGDPFDIRTEQGP 355
Cdd:PRK11809 890 MIVDSSALTEQVVADVLASAFDSAGQRCSAlrvlclqddvADRTL-------KMLRGAMaECR----MGNPDRLSTDIGP 958
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 356 QIDQKQFDKILDLIESGKKEGAK---LECGGSAMEDRGLFIKPTVFsEVTDTMRIaKEEIFGPVQPILKFK--NIEEVIK 430
Cdd:PRK11809 959 VIDAEAKANIERHIQAMRAKGRPvfqAARENSEDWQSGTFVPPTLI-ELDSFDEL-KREVFGPVLHVVRYNrnQLDELIE 1036
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 431 RANSLEYGLTAAVFTKNLDKALKLASALESGTVWINcYNAIYA----QaPFGGFKMSGNG 486
Cdd:PRK11809 1037 QINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAvvgvQ-PFGGEGLSGTG 1094
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
71-466 |
9.40e-39 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 146.61 E-value: 9.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 71 VDKAVEAAHAAfqrGSPWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPFLHAFFIDleGCIKTLRYFA--GWA 148
Cdd:cd07084 1 PERALLAADIS---TKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENIC--GDQVQLRARAfvIYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 149 DKIQGRTIPTDDNVVCFTRHE---PIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVG- 224
Cdd:cd07084 76 YRIPHEPGNHLGQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 225 FPPGVVNIVPGFGPTvGAAISSHPHISKIAFTGSTEVGklvkeAASRSNLK--RVTLELGGKNPCIVCADADL--DLAVE 300
Cdd:cd07084 156 LPPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVA-----EKLALDAKqaRIYLELAGFNWKVLGPDAQAvdYVAWQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 301 CAhQGVFFNQGQCCTAASRVFVEEQiyPEfVRRSVEYAKKRpigdpFDIRTEQGPQIDQKQFDKILDLIES-GKKEGAKL 379
Cdd:cd07084 230 CV-QDMTACSGQKCTAQSMLFVPEN--WS-KTPLVEKLKAL-----LARRKLEDLLLGPVQTFTTLAMIAHmENLLGSVL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 380 ECGGSAM------EDRGLFIKPTVF---SEVTDTMRIAKEEIFGPVQPILKFKNIEE--VIKRANSLEYGLTAAVFTKNL 448
Cdd:cd07084 301 LFSGKELknhsipSIYGACVASALFvpiDEILKTYELVTEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDP 380
|
410
....*....|....*....
gi 1952740663 449 DKALKLASALES-GTVWIN 466
Cdd:cd07084 381 IFLQELIGNLWVaGRTYAI 399
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
169-504 |
3.21e-38 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 146.02 E-value: 3.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 169 EPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGfGPTVGAAISSHP 248
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKY-LDSKAVKVIEG-GPAVGEQLLQHK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 249 HiSKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIV-CADA--DLDLAVE---------CAhqgvffnqGQCCTA 316
Cdd:PLN02203 185 W-DKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIVdSLSSsrDTKVAVNrivggkwgsCA--------GQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 317 ASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRTeQGPQIDQKQFDKILDLIESgKKEGAKLECGGSAMEDRgLFIKPT 396
Cdd:PLN02203 255 IDYVLVEERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLLKD-PRVAASIVHGGSIDEKK-LFIEPT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 397 VFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASALESGTVWINCYNAIYA--Q 474
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYAcdS 411
|
330 340 350
....*....|....*....|....*....|
gi 1952740663 475 APFGGFKMSGNGRELGEYALAEYTEVKTVT 504
Cdd:PLN02203 412 LPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
121-503 |
2.93e-34 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 134.79 E-value: 2.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 121 DTGKPFLHAFFID---LEGCIK-TLRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALC 196
Cdd:PLN02174 59 DLGKPELESSVYEvslLRNSIKlALKQLKNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAIS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 197 CGNTIVVKPAEQTPLTALYLGSLIKEVgFPPGVVNIVPGFGPTVGAAISShpHISKIAFTGSTEVGKLVKEAASRsNLKR 276
Cdd:PLN02174 139 AGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALLEQ--KWDKIFYTGSSKIGRVIMAAAAK-HLTP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 277 VTLELGGKNPCIVCADADLDLAVECAHQGVF-FNQGQCCTAASRVFVEEQIYPEFVRRSVEYAKKRPIGDPFDIRtEQGP 355
Cdd:PLN02174 215 VVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESK-DMSR 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 356 QIDQKQFDKILDLIESgKKEGAKLECGGSamEDR-GLFIKPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVIKRANS 434
Cdd:PLN02174 294 IVNSTHFDRLSKLLDE-KEVSDKIVYGGE--KDReNLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRS 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952740663 435 LEYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNAIYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 503
Cdd:PLN02174 371 RPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiAVHLALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
35-459 |
4.90e-29 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 120.19 E-value: 4.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 35 FINNEWHESkSGKKFATYNPSTLEKICEVEeGDKLDVDKAVeaAHAAFQRGSPWRRLDALGRGWLLHQLADLVERDRAIL 114
Cdd:PRK11903 8 YVAGRWQAG-SGAGTPLFDPVTGEELVRVS-ATGLDLAAAF--AFAREQGGAALRALTYAQRAALLAAIVKVLQANRDAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 115 ATLETMDTGKPFLHAFFiDLEGCIKTLRYFAGWADKIQGRTIPTDDNVVCFTRHEPI----------GVCGAITPWNFPL 184
Cdd:PRK11903 84 YDIATANSGTTRNDSAV-DIDGGIFTLGYYAKLGAALGDARLLRDGEAVQLGKDPAFqgqhvlvptrGVALFINAFNFPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 185 LMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVG-FPPGVVNIVPGFGPTVGAAISShphISKIAFTGSTEVGK 263
Cdd:PRK11903 163 WGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLDHLQP---FDVVSFTGSAETAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 264 LVKE--AASRSNLkRVTLELGGKNPCIVCADAD-----LDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVE 336
Cdd:PRK11903 240 VLRShpAVVQRSV-RVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 337 YAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIEsGKKEGAKLECGGSAME------DRGLFIKPTVF--SEVTDTMRIA 408
Cdd:PRK11903 319 RLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFAlvdadpAVAACVGPTLLgaSDPDAATAVH 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1952740663 409 KEEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKnlDKALKLASALE 459
Cdd:PRK11903 398 DVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSD--DAAFLAAAALE 446
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
35-458 |
1.22e-24 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 106.97 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 35 FINNEWHESkSGKKFATYNPSTLEKICEVEeGDKLDVDKAVEAAHaafQRGSP-WRRLDALGRGWLLHQLAD-LVERDRA 112
Cdd:cd07128 4 YVAGQWHAG-TGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYAR---EKGGPaLRALTFHERAAMLKALAKyLMERKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 113 ILATleTMDTGKPFLHAFfIDLEGCIKTLRYFAGwadkiQGRTIPTDDNV-------------------VCFTRHepiGV 173
Cdd:cd07128 79 LYAL--SAATGATRRDSW-IDIDGGIGTLFAYAS-----LGRRELPNAHFlvegdveplskdgtfvgqhILTPRR---GV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 174 CGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVG-FPPGVVNIVPGfgpTVGAAISSHPHISK 252
Cdd:cd07128 148 AVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG---SVGDLLDHLGEQDV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 253 IAFTGSTEVG-KLVKEAASRSNLKRVTLELGGKNPCIVCADA-----DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQI 326
Cdd:cd07128 225 VAFTGSAATAaKLRAHPNIVARSIRFNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEAR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 327 YPEFVRRSVEYAKKRPIGDPFDIRTEQGPQIDQKQFDKILDLIESGKKEGAKLECGGSAME------DRGLFIKPTVF-- 398
Cdd:cd07128 305 VDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEvvgadaEKGAFFPPTLLlc 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952740663 399 ------SEVTDTmriakeEIFGPVQPILKFKNIEEVIKRANSLEYGLTAAVFTKNLDKALKLASAL 458
Cdd:cd07128 385 ddpdaaTAVHDV------EAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGA 444
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
71-459 |
1.33e-20 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 94.15 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 71 VDKAVEAAHAAFQrgsPWRRLDALGRGWLLHQLADLVERDRAILATLETMDTGKPflhaffidlEGCI-----KT---LR 142
Cdd:cd07129 1 VDAAAAAAAAAFE---SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLP---------EARLqgelgRTtgqLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 143 YFA------GWADKI------QGRTIPTDDNVVCFTRHEPIGVCGAItpwNFPLLMLVW--KLAPALCCGNTIVVKPAEQ 208
Cdd:cd07129 69 LFAdlvregSWLDARidpadpDRQPLPRPDLRRMLVPLGPVAVFGAS---NFPLAFSVAggDTASALAAGCPVVVKAHPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 209 TPLTALYLGSLIKEV----GFPPGVVNIVPGFGPTVGAAISSHPHISKIAFTGSTEVGK-LVKEAASRSNLKRVTLELGG 283
Cdd:cd07129 146 HPGTSELVARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRaLFDAAAARPEPIPFYAELGS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 284 KNPCIVCADADLDLAVECAhQG----VFFNQGQCCTAASRVFV-EEQIYPEFVRRSVEYAKKRPIGdpfdirTEQGPQId 358
Cdd:cd07129 226 VNPVFILPGALAERGEAIA-QGfvgsLTLGAGQFCTNPGLVLVpAGPAGDAFIAALAEALAAAPAQ------TMLTPGI- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 359 QKQFDKILDLIESGKkeGAKLECGGSAMEDRGLFiKPTVFSEVTDTMR---IAKEEIFGPVQPILKFKNIEEVIKRANSL 435
Cdd:cd07129 298 AEAYRQGVEALAAAP--GVRVLAGGAAAEGGNQA-APTLFKVDAAAFLadpALQEEVFGPASLVVRYDDAAELLAVAEAL 374
|
410 420
....*....|....*....|....*.
gi 1952740663 436 EYGLTAAVF--TKNLDKALKLASALE 459
Cdd:cd07129 375 EGQLTATIHgeEDDLALARELLPVLE 400
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
100-479 |
1.69e-17 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 84.58 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 100 LHQLADLVERDRAILATLETMDTGKPF--LHAFFIDLEGCIK--------TLRYFAGWADKIQGRTIPtdDNVVCFTRHE 169
Cdd:cd07077 22 INAIANALYDTRQRLASEAVSERGAYIrsLIANWIAMMGCSEsklyknidTERGITASVGHIQDVLLP--DNGETYVRAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 170 PIGVCGAITPWNFPLLMlVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEV---GFPPGVVNIVPGFGPTVGAAISS 246
Cdd:cd07077 100 PIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPHPSDELAEELLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 247 HPHISKIAFTGSTEVgklVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCctaasrvFVEEQI 326
Cdd:cd07077 179 HPKIDLIVATGGRDA---VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQNAC-------ASEQNL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 327 YpefVRRSVEYAKKRPIgdpfdirteqgpqidqkqfdkILDLIESGKK--EGAKLecggsamedrglfikptVFSEVTDT 404
Cdd:cd07077 249 Y---VVDDVLDPLYEEF---------------------KLKLVVEGLKvpQETKP-----------------LSKETTPS 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952740663 405 MRIAKEEIFGPVQPILKFKNIEEVIKRANSL--EYG--LTAAVFTKNLDKALKLASALESGTVWINCYNAIYAQAPFGG 479
Cdd:cd07077 288 FDDEALESMTPLECQFRVLDVISAVENAWMIieSGGgpHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAGK 366
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
70-459 |
1.60e-15 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 78.43 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 70 DVDKAVEAAHAAFQRgspwrrldalgrgwllHQLADLVERDRAILATLETmdtgkpflhaffidlegCIKTLRYFAGWA- 148
Cdd:cd07121 5 TVDDAVAAAKAAQKQ----------------YRKCTLADREKIIEAIREA-----------------LLSNAEELAEMAv 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 149 ---------DKI-----QGRTIP----------TDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVK 204
Cdd:cd07121 52 eetgmgrveDKIaknhlAAEKTPgtedltttawSGDNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFN 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 205 PAEQTPLTALYLGSL----IKEVGFPPGVVNIVPGfgPTVGAA--ISSHPHISKIAFTGSTEVGKlvkeaASRSNLKRVT 278
Cdd:cd07121 132 PHPGAKKVSAYAVELinkaIAEAGGPDNLVVTVEE--PTIETTneLMAHPDINLLVVTGGPAVVK-----AALSSGKKAI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 279 LELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRSVEyakkrpigdpfdirtEQGPQID 358
Cdd:cd07121 205 GAGAGNPPVVVDETADIEKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQR---------------NGAYVLN 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 359 QKQFDKILDLIESGKKEGA---KLEcGGSA---MEDRGLFIKPT---VFSEVTDTMRIAKEEIFGPVQPILKFKNIEEVI 429
Cdd:cd07121 270 DEQAEQLLEVVLLTNKGATpnkKWV-GKDAskiLKAAGIEVPADirlIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAI 348
|
410 420 430
....*....|....*....|....*....|..
gi 1952740663 430 KRANSLEYGL--TAAVFTKNLDKALKLASALE 459
Cdd:cd07121 349 ELAVELEHGNrhTAIIHSKNVENLTKMARAMQ 380
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
70-459 |
4.07e-15 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 77.64 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 70 DVDKAVEAAHAAFQRgspwrrldalgrgwllHQLADLVERDRAI-------------LATLETMDTGKpflhaffidleG 136
Cdd:PRK15398 37 SVDDAVAAAKVAQQR----------------YQQKSLAMRQRIIdaireallphaeeLAELAVEETGM-----------G 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 137 ciktlRYfagwADKI-----QGRTIP----------TDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTI 201
Cdd:PRK15398 90 -----RV----EDKIaknvaAAEKTPgvedlttealTGDNGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 202 VVKPAEQTPLTALYLGSL----IKEVGFPPGVVNIVPGfgPTVGAA--ISSHPHISKIAFTGstevGKLVKEAASRSNlK 275
Cdd:PRK15398 161 VFSPHPGAKKVSLRAIELlneaIVAAGGPENLVVTVAE--PTIETAqrLMKHPGIALLVVTG----GPAVVKAAMKSG-K 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 276 RVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQIYPEFVRRsveyakkrpigdpfdIRTEQGP 355
Cdd:PRK15398 234 KAIGAGAGNPPVVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRL---------------MEKNGAV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 356 QIDQKQFDKILDLIESGKKEGAKLECGGSA---MEDRGLFIKPTV---FSEVTDTMRIAKEEIFGPVQPILKFKNIEEVI 429
Cdd:PRK15398 299 LLTAEQAEKLQKVVLKNGGTVNKKWVGKDAakiLEAAGINVPKDTrllIVETDANHPFVVTELMMPVLPVVRVKDVDEAI 378
|
410 420 430
....*....|....*....|....*....|..
gi 1952740663 430 KRANSLEYGL--TAAVFTKNLDKALKLASALE 459
Cdd:PRK15398 379 ALAVKLEHGNrhTAIMHSRNVDNLNKMARAIQ 410
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
170-443 |
2.05e-13 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 72.53 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 170 PIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKPAEQTPLTALYLGSLIKEVGFPPGVVNIVPGFGPTVGAAIS-SHP 248
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLeANP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 249 HIskIAFTGSTEVGklvkEAASRSNLKRVTLELGGKNPCIVCAD-ADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQ-I 326
Cdd:cd07126 222 RM--TLFTGSSKVA----ERLALELHGKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 327 YPEFVRRSVEYAKKRPIGDpfdirTEQGP------QIDQKQFDKILDLiesgkkEGAKLECGGS------------AMED 388
Cdd:cd07126 296 QAGILDKLKALAEQRKLED-----LTIGPvltwttERILDHVDKLLAI------PGAKVLFGGKpltnhsipsiygAYEP 364
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952740663 389 RGLFIkPTVFSEVTDTMRIAKEEIFGPVQPILKFKNIEE--VIKRANSLEYGLTAAV 443
Cdd:cd07126 365 TAVFV-PLEEIAIEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAV 420
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
159-482 |
6.82e-10 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 61.13 E-value: 6.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 159 DDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKP----AEQTPLTALYLGSLIKEVGFPPGVVNIVP 234
Cdd:cd07081 84 DENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWID 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 235 GFGPTVGAAISSHPHISKIAFTGstevGKLVKEAAsRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCC 314
Cdd:cd07081 164 NPSIELAQRLMKFPGIGLLLATG----GPAVVKAA-YSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVIC 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 315 TAASRVFVEEQIYPEFVRRsveyakkrpigdpfdIRTEQGPQIDQKQFDKILDLIES---------GKKEGAKLECGGSA 385
Cdd:cd07081 239 ASEQSVIVVDSVYDEVMRL---------------FEGQGAYKLTAEELQQVQPVILKngdvnrdivGQDAYKIAAAAGLK 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 386 M--EDRGLFIKPTVFSEvtdtMRIAKEEIFGPVQPILKFKNIEEVIKRANSLEY----GLTAAVFTKNL---DKALKLAS 456
Cdd:cd07081 304 VpqETRILIGEVTSLAE----HEPFAHEKLSPVLAMYRAANFADADAKALALKLeggcGHTSAMYSDNIkaiENMNQFAN 379
|
330 340
....*....|....*....|....*.
gi 1952740663 457 ALESGTVWINCYNAIYAQAPFGGFKM 482
Cdd:cd07081 380 AMKTSRFVKNGPCSQGGLGDLYNFRG 405
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
67-372 |
6.86e-08 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 55.18 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 67 DKLDVDKAVEAAHAAFQRgspWRRLDALGR-GWLLHQLADLVERDRAIL-ATLETmdTGKPFLHAFFID----LEGCIKT 140
Cdd:cd07127 82 PQCDPDALLAAARAAMPG---WRDAGARARaGVCLEILQRLNARSFEMAhAVMHT--TGQAFMMAFQAGgphaQDRGLEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 141 LRYfagwADKIQGRTIPTDDNVVCFTRHEPI-----------GV-----CGAITPWN-FPLLMlvwklaPALCCGNTIVV 203
Cdd:cd07127 157 VAY----AWREMSRIPPTAEWEKPQGKHDPLamektftvvprGValvigCSTFPTWNgYPGLF------ASLATGNPVIV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 204 KPAeqtPLTALYLGSLIK-------EVGFPPGVVNIV---PGFGptVGAAISSHPHISKIAFTGSTEVGKLVKEAASRsn 273
Cdd:cd07127 227 KPH---PAAILPLAITVQvarevlaEAGFDPNLVTLAadtPEEP--IAQTLATRPEVRIIDFTGSNAFGDWLEANARQ-- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 274 lKRVTLELGGKNPCIVcaDADLDLAVECAHQGVFFN--QGQCCTAASRVFVeeqiypefvrrsveyakkrpigdPFD-IR 350
Cdd:cd07127 300 -AQVYTEKAGVNTVVV--DSTDDLKAMLRNLAFSLSlySGQMCTTPQNIYV-----------------------PRDgIQ 353
|
330 340
....*....|....*....|..
gi 1952740663 351 TEQGpqidQKQFDKILDLIESG 372
Cdd:cd07127 354 TDDG----RKSFDEVAADLAAA 371
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
169-467 |
5.81e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 51.72 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 169 EPIGVCGAITPWNFPLLMLVWKLAPALCCGNTIVVKP----AEQTPLTALYLGSLIKEVGFPPGVVNIVPgfGPTVGA-- 242
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhpraKKCSIEAAKIMREAAVAAGAPEGLIQWIE--EPSIELtq 171
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 243 AISSHPHISKIAFTGStevGKLVKEAASRSnlkrvTLELG---GKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASR 319
Cdd:cd07122 172 ELMKHPDVDLILATGG---PGMVKAAYSSG-----KPAIGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQS 243
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 320 VFVEEQIYPEFVRRSVeyakkrpigdpfdirtEQGPQI----DQKQFDKILdLIESGK-------KEGAKL--ECGGSAM 386
Cdd:cd07122 244 VIVDDEIYDEVRAELK----------------RRGAYFlneeEKEKLEKAL-FDDGGTlnpdivgKSAQKIaeLAGIEVP 306
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952740663 387 EDRGLFIKPtvFSEVTDTMRIAKEEIFgPVQPILKFKNIEEVIKRANS-LEY---GLTAAVFTKNLDKALKLASALESGT 462
Cdd:cd07122 307 EDTKVLVAE--ETGVGPEEPLSREKLS-PVLAFYRAEDFEEALEKARElLEYggaGHTAVIHSNDEEVIEEFALRMPVSR 383
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....*
gi 1952740663 463 VWINC 467
Cdd:cd07122 384 ILVNT 388
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