|
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 ... |
26-399 |
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: 683.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 26 NLEVKFTKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGSPWRRLDALSRGRLLHQLAD 105
Cdd:cd07141 1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 106 LVERDRATLA---------------------------------------------------------------------- 115
Cdd:cd07141 81 LIERDRAYLAsletldngkpfsksylvdlpgaikvlryyagwadkihgktipmdgdfftytrhepvgvcgqiipwnfpll 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 -------------------------------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLV 158
Cdd:cd07141 161 maawklapalacgntvvlkpaeqtpltalylaslikeAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 159 KEAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGD 238
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 239 PFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSI 318
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 319 EEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
.
gi 658310017 399 K 399
Cdd:cd07141 481 K 481
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
32-398 |
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: 597.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 32 TKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGSpWRRLDALSRGRLLHQLADLVERDR 111
Cdd:cd07091 4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIERDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 112 ATLA---------------------------------------------------------------------------- 115
Cdd:cd07091 83 DELAalesldngkpleesakgdvalsikclryyagwadkiqgktipidgnflaytrrepigvcgqiipwnfpllmlawkl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 -------------------------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASR 164
Cdd:cd07091 163 apalaagntvvlkpaeqtplsalylaelikeAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 165 SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKT 244
Cdd:cd07091 243 SNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 245 EQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKR 324
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIER 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658310017 325 ANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07091 403 ANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
29-396 |
1.37e-174 |
|
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: 495.86 E-value: 1.37e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 29 VKFTKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGsPWRRLDALSRGRLLHQLADLVE 108
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 109 RDRATLA------------------------------------------------------------------------- 115
Cdd:cd07142 80 KHADELAaletwdngkpyeqaryaevplaarlfryyagwadkihgmtlpadgphhvytlhepigvvgqiipwnfpllmfa 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 ----------------------------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEA 161
Cdd:cd07142 160 wkvgpalacgntivlkpaeqtplsallaaklaaeAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 162 ASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFD 241
Cdd:cd07142 240 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 242 VKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEV 321
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658310017 322 IKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 396
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
32-400 |
3.65e-168 |
|
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: 479.62 E-value: 3.65e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 32 TKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQrgsPWRRLDALSRGRLLHQLADLVERDR 111
Cdd:COG1012 6 YPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 112 ATLA---------------------------------------------------------------------------- 115
Cdd:COG1012 83 EELAalltletgkplaeargevdraadflryyagearrlygetipsdapgtrayvrreplgvvgaitpwnfplalaawkl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 -------------------------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASR 164
Cdd:COG1012 163 apalaagntvvlkpaeqtplsalllaelleeAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 165 sNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKT 244
Cdd:COG1012 243 -NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 245 EQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMED-KGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIK 323
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658310017 324 RANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALY-AQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 400
Cdd:COG1012 402 LANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
19-405 |
1.25e-164 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 472.76 E-value: 1.25e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 19 ALPRPIR-NLEVKFTKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGsPWRRLDALSRG 97
Cdd:PLN02466 44 AVEEPITpPVQVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEG-PWPKMTAYERS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 98 RLLHQLADLVERDRATLA-------------------------------------------------------------- 115
Cdd:PLN02466 123 RILLRFADLLEKHNDELAaletwdngkpyeqsakaelpmfarlfryyagwadkihgltvpadgphhvqtlhepigvagqi 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 ---------------------------------------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTG 150
Cdd:PLN02466 203 ipwnfpllmfawkvgpalacgntivlktaeqtplsalyaakllheAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 151 STEVGKLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEY 230
Cdd:PLN02466 283 STDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKAR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 231 AKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQ 310
Cdd:PLN02466 363 ALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQ 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 311 PILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEY 390
Cdd:PLN02466 443 SILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNY 522
|
490
....*....|....*
gi 658310017 391 TEVKTVTIKLgdKNP 405
Cdd:PLN02466 523 LQVKAVVTPL--KNP 535
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
45-396 |
7.10e-163 |
|
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: 465.47 E-value: 7.10e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 45 SGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQrgsPWRRLDALSRGRLLHQLADLVERDRATLA--------- 115
Cdd:pfam00171 5 ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAeletlengk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 --------------------------------------------------------------------------------
Cdd:pfam00171 82 plaeargevdraidvlryyaglarrldgetlpsdpgrlaytrreplgvvgaitpwnfplllpawkiapalaagntvvlkp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 -----------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKN 178
Cdd:pfam00171 162 seltpltalllaelfeeAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTLELGGKN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 179 PCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKI 258
Cdd:pfam00171 241 PLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 259 LELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFT 338
Cdd:pfam00171 321 LKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFT 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 658310017 339 KNLDKALKLASALESGTVWINCYNALYA-QAPFGGFKMSGNGRELGEYALAEYTEVKTV 396
Cdd:pfam00171 401 SDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
32-400 |
2.49e-162 |
|
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: 464.69 E-value: 2.49e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 32 TKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQrgSPWRR-LDALSRGRLLHQLADLVERD 110
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWGLkVSGSKRGRCLSKLADLMERN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 111 RATLA--------------------------------------------------------------------------- 115
Cdd:cd07143 85 LDYLAsiealdngktfgtakrvdvqasadtfryyggwadkihgqvietdikkltytrhepigvcgqiipwnfpllmcawk 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 --------------------------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAAS 163
Cdd:cd07143 165 iapalaagntivlkpseltplsalymtklipeAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 164 RSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVK 243
Cdd:cd07143 245 KSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 244 TEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIK 323
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIK 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658310017 324 RANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 400
Cdd:cd07143 405 RANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
28-402 |
4.06e-156 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 449.66 E-value: 4.06e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 28 EVKFTKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGsPWRRLDALSRGRLLHQLADLV 107
Cdd:PLN02766 17 EIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 108 ERDRATLA------------------------------------------------------------------------ 115
Cdd:PLN02766 96 EEHIEELAaldtidagklfalgkavdipaaagllryyagaadkihgetlkmsrqlqgytlkepigvvghiipwnfpstmf 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 -----------------------------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKE 160
Cdd:PLN02766 176 fmkvapalaagctmvvkpaeqtplsalfyahlaklAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 161 AASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPF 240
Cdd:PLN02766 256 AAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 241 DVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEE 320
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 321 VIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 400
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPL 495
|
..
gi 658310017 401 GD 402
Cdd:PLN02766 496 YN 497
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
32-400 |
7.34e-154 |
|
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: 443.39 E-value: 7.34e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 32 TKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQrgSPWRRLDALSRGRLLHQLADLVERDR 111
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEKNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 112 ATLA---------------------------------------------------------------------------- 115
Cdd:cd07144 86 DLLAaiealdsgkpyhsnalgdldeiiaviryyagwadkiqgktiptspnklaytlhepygvcgqiipwnyplamaawkl 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 -------------------------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASr 164
Cdd:cd07144 166 apalaagntvvikpaentplsllyfanlvkeAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 165 SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKR-PVGDPFDVK 243
Cdd:cd07144 245 QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 244 TEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMED---KGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEE 320
Cdd:cd07144 325 TVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEglgKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 321 VIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 400
Cdd:cd07144 405 AIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHINL 484
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
103-398 |
1.46e-151 |
|
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: 435.48 E-value: 1.46e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 103 LADLVERdratlaAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIV 182
Cdd:cd07078 142 LAELLAE------AGLPPGVLNVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIV 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 183 CADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELI 262
Cdd:cd07078 215 FDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 263 ESGKKEGAKLECGGSAME-DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNL 341
Cdd:cd07078 295 EDAKAEGAKLLCGGKRLEgGKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 658310017 342 DKALKLASALESGTVWINCYNA-LYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07078 375 ERALRVAERLEAGTVWINDYSVgAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
35-400 |
3.16e-142 |
|
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: 413.63 E-value: 3.16e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 35 FINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGsPWRRLDALSRGRLLHQLADLVERDRATL 114
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSG-EWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 115 A------------------------------------------------------------------------------- 115
Cdd:cd07119 80 Arletlntgktlreseididdvancfryyaglatketgevydvpphvisrtvrepvgvcglitpwnypllqaawklapal 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 ---------------------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLK 168
Cdd:cd07119 160 aagntvvikpsevtplttialfelieeAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 169 RVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGP 248
Cdd:cd07119 239 KVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 249 QIDQKQFDKILELIESGKKEGAKLECGGSAMED----KGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKR 324
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658310017 325 ANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 400
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININL 474
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
46-398 |
7.28e-140 |
|
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: 406.99 E-value: 7.28e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 46 GKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGSpWRRLDALSRGRLLHQLADLVERDRATLA---------- 115
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELAlletldmgkp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 --------------------------------------------------------------------------------
Cdd:cd07112 80 isdalavdvpsaantfrwyaeaidkvygevaptgpdalalitreplgvvgavvpwnfpllmaawkiapalaagnsvvlkp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 -----------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGKN 178
Cdd:cd07112 160 aeqspltalrlaelaleAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 179 PCIVCADA-DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDK 257
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 258 ILELIESGKKEGAKLECGGSA--MEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAA 335
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658310017 336 VFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
51-398 |
5.17e-137 |
|
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: 399.25 E-value: 5.17e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 51 TCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLA--------------- 115
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG---WSRMSPAERARILHKVADLIEARADELAllesldtgkpitlar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 --------------------------------------------------------------------------------
Cdd:cd07093 78 trdipraaanfrffadyilqldgesypqdggalnyvlrqpvgvaglitpwnlplmlltwkiapalafgntvvlkpsewtp 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 ------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVC 183
Cdd:cd07093 158 ltawllaelaneAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 184 ADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIE 263
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 264 SGKKEGAKLECGGSAME----DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTK 339
Cdd:cd07093 317 LARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 658310017 340 NLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
53-398 |
1.67e-136 |
|
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: 398.08 E-value: 1.67e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFqRGSPWRRLDALSRGRLLHQLADLVERDRATLA----------------- 115
Cdd:cd07114 3 NPATGEPWARVPEASAADVDRAVAAARAAF-EGGAWRKLTPTERGKLLRRLADLIEANAEELAeletrdngkliretraq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 --------------------------------------------------------------------------------
Cdd:cd07114 82 vrylaewyryyagladkiegavipvdkgdylnftrreplgvvaaitpwnspllllakklapalaagntvvlkpsehtpas 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 ----------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCAD 185
Cdd:cd07114 162 tlelaklaeeAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 186 ADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESG 265
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 266 KKEGAKLECGGSAME----DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNL 341
Cdd:cd07114 321 REEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDL 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 658310017 342 DKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07114 401 ARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
34-397 |
1.17e-133 |
|
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: 391.10 E-value: 1.17e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 34 IFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAF---QRGSPWRRLDALSRGRLLHQ-----LAD 105
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFpawSATSVEERAALLERIAEAYEaradeLAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 106 LV-----------------------------------ERDR-------------------------------ATLAAG-- 117
Cdd:cd07138 81 AItlemgapitlaraaqvglgighlraaadalkdfefEERRgnslvvrepigvcglitpwnwplnqivlkvaPALAAGct 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 118 ------------------------FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSnLKRVTLE 173
Cdd:cd07138 161 vvlkpsevaplsaiilaeildeagLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADT-VKRVALE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 174 LGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQK 253
Cdd:cd07138 240 LGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 254 QFDKILELIESGKKEGAKLECGGS---AMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDY 330
Cdd:cd07138 320 QFDRVQGYIQKGIEEGARLVAGGPgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPY 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658310017 331 GLTAAVFTKNLDKALKLASALESGTVWINcYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 397
Cdd:cd07138 400 GLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
28-399 |
3.75e-131 |
|
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: 385.70 E-value: 3.75e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 28 EVKF-TKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGsPWRRLDALSRGRLLHQLADL 106
Cdd:cd07140 1 TLKMpHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENG-EWGKMNARDRGRLMYRLADL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 107 VERDRATLA----------------------------------------------------------------------- 115
Cdd:cd07140 80 MEEHQEELAtiesldsgavytlalkthvgmsiqtfryfagwcdkiqgktipinqarpnrnltltkrepigvcgivipwny 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 ----------------------------------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVG 155
Cdd:cd07140 160 plmmlawkmaaclaagntvvlkpaqvtpltalkfaeltvkAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 156 KLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRP 235
Cdd:cd07140 240 KHIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 236 VGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKF 315
Cdd:cd07140 320 IGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 316 KS--IEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEV 393
Cdd:cd07140 400 DDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKT 479
|
....*.
gi 658310017 394 KTVTIK 399
Cdd:cd07140 480 KTVTIE 485
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
51-400 |
2.30e-130 |
|
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: 382.56 E-value: 2.30e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 51 TCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQrgsPWRRLDALSRGRLLHQLADLVERDRATLA--------------- 115
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELArlesldtgkpiraar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 --------------------------------------------------------------------------------
Cdd:cd07115 78 rldvpraadtfryyagwadkiegevipvrgpflnytvrepvgvvgaivpwnfplmfaawkvapalaagntvvlkpaeltp 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 ------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCIVC 183
Cdd:cd07115 158 lsalriaelmaeAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 184 ADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIE 263
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 264 SGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDK 343
Cdd:cd07115 317 VGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 658310017 344 ALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 400
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
53-398 |
1.16e-127 |
|
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: 375.23 E-value: 1.16e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLA----------------- 115
Cdd:cd07103 3 NPATGEVIGEVPDAGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLArlltleqgkplaearge 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 --------------------------------------------------------------------------------
Cdd:cd07103 80 vdyaasflewfaeearriygrtipspapgkrilvikqpvgvvaaitpwnfpaamitrkiapalaagctvvlkpaeetpls 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 ----------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCIVCAD 185
Cdd:cd07103 160 alalaelaeeAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPFIVFDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 186 ADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESG 265
Cdd:cd07103 239 ADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 266 KKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKAL 345
Cdd:cd07103 319 VAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 658310017 346 KLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07103 399 RVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
65-398 |
1.24e-127 |
|
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: 375.52 E-value: 1.24e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 65 EGDKPDVDKAVEAAQVAFQRGsPWRRLDALSRGRLLHQLADLVERDRATLA----------------------------- 115
Cdd:cd07118 15 EGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLAlietlesgkpisqargeiegaadlwryaa 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 ------------------------------------------------------------------------------AG 117
Cdd:cd07118 94 slartlhgdsynnlgddmlglvlrepigvvgiitpwnfpflilsqklpfalaagctvvvkpseftsgttlmlaellieAG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 118 FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQ 197
Cdd:cd07118 174 LPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFADADLDAAADAVVF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 198 GVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGS 277
Cdd:cd07118 253 GVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 278 AMED-KGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTV 356
Cdd:cd07118 333 RLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTV 412
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 658310017 357 WINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07118 413 WVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
103-398 |
3.57e-124 |
|
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: 365.70 E-value: 3.57e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 103 LADLVErdratlAAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIV 182
Cdd:cd07104 145 IAEIFE------EAGLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 183 CADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELI 262
Cdd:cd07104 218 LDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIV 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 263 ESGKKEGAKLECGGSAmedKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLD 342
Cdd:cd07104 298 EDAVAAGARLLTGGTY---EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLE 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 658310017 343 KALKLASALESGTVWINCYNAL-YAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07104 375 RAMAFAERLETGMVHINDQTVNdEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
35-402 |
5.28e-123 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 364.97 E-value: 5.28e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 35 FINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLV-ERDR-- 111
Cdd:PRK13252 10 YIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVDILrERNDel 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 112 ------------------------------ATLA---------------------------------------------- 115
Cdd:PRK13252 87 aaletldtgkpiqetsvvdivtgadvleyyAGLApalegeqiplrggsfvytrreplgvcagigawnypiqiacwksapa 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 ----------------------------AGFPPGVVNIVPGFGPtVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSnL 167
Cdd:PRK13252 167 laagnamifkpsevtpltalklaeiyteAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS-L 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 168 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQG 247
Cdd:PRK13252 245 KEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 248 PQIDQKQFDKILELIESGKKEGAKLECGGSAME----DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIK 323
Cdd:PRK13252 325 PLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTeggfANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIA 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658310017 324 RANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLGD 402
Cdd:PRK13252 405 RANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVEMGP 483
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
33-400 |
1.23e-121 |
|
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: 361.28 E-value: 1.23e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 33 KIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERD-- 110
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT---WGKTSVAERANILNKIADRIEENle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 111 --------------RAT--------------------------------------------------------------- 113
Cdd:cd07559 79 llavaetldngkpiRETlaadiplaidhfryfagviraqegslseidedtlsyhfheplgvvgqiipwnfpllmaawkla 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 114 --LAAG-------------------------FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsN 166
Cdd:cd07559 159 paLAAGntvvlkpasqtplsilvlmeligdlLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE-N 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 167 LKRVTLELGGKNPCIVCADA-----DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFD 241
Cdd:cd07559 238 LIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 242 VKTEQGPQIDQKQFDKILELIESGKKEGAKLECGG----SAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKS 317
Cdd:cd07559 318 PETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGerltLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 318 IEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 397
Cdd:cd07559 398 EEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNIL 477
|
...
gi 658310017 398 IKL 400
Cdd:cd07559 478 VSY 480
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
53-398 |
4.61e-120 |
|
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: 355.68 E-value: 4.61e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLA----------------- 115
Cdd:cd07106 3 NPATGEVFASAPVASEAQLDQAVAAAKAAFPG---WSATPLEERRAALLAIADAIEANAEELArlltleqgkplaeaqfe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 -------------------------------------------------------------AG----------------- 117
Cdd:cd07106 80 vggavawlrytasldlpdeviedddtrrvelrrkplgvvaaivpwnfplllaawkiapallAGntvvlkpspftplctlk 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 118 --------FPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCIVCADADLD 189
Cdd:cd07106 160 lgelaqevLPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAA-KTLKRVTLELGGNDAAIVLPDVDID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 190 LAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEG 269
Cdd:cd07106 238 AVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 270 AKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLAS 349
Cdd:cd07106 318 AKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVAR 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 658310017 350 ALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07106 398 RLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
53-401 |
1.16e-117 |
|
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: 350.07 E-value: 1.16e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLA----------------- 115
Cdd:cd07090 3 EPATGEVLATVHCAGAEDVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIArletidngkpieearvd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 --------------------------------------------------------------------------------
Cdd:cd07090 80 idssadcleyyaglaptlsgehvplpggsfaytrreplgvcagigawnypiqiaswksapalacgnamvykpspftplta 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 ---------AGFPPGVVNIVPGFGPTvGAAISSHPQINKIAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCIVCADA 186
Cdd:cd07090 160 lllaeilteAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 187 DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGK 266
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 267 KEGAKLECGGS--AMEDK---GLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNL 341
Cdd:cd07090 318 QEGAKVLCGGErvVPEDGlenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDL 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 342 DKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLG 401
Cdd:cd07090 398 QRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEMG 457
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
35-398 |
2.38e-116 |
|
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: 347.33 E-value: 2.38e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 35 FINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAfQRGspWRRLDALSRGRLLHQLADLVERDRATL 114
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAA-QKA--WERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 115 A------------------------------------------------------------------------------- 115
Cdd:cd07088 78 Akliveeqgktlslarveveftadyidymaewarriegeiipsdrpnenififkvpigvvagilpwnfpffliarklapa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 ----------------------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNL 167
Cdd:cd07088 158 lvtgntivikpseetplnalefaelvdeAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-NI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 168 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQG 247
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 248 PQIDQKQFDKILELIESGKKEGAKLECGGSAME-DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRAN 326
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAN 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658310017 327 STDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07088 397 DSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
33-400 |
1.16e-115 |
|
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: 345.59 E-value: 1.16e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 33 KIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERD-- 110
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT---WRKTTVAERANILNKIADIIDENke 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 111 --------------RAT--------------------------------------------------------------- 113
Cdd:cd07117 79 llamvetldngkpiRETravdiplaadhfryfagviraeegsanmidedtlsivlrepigvvgqiipwnfpflmaawkla 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 114 --LAAG-------------------------FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsN 166
Cdd:cd07117 159 paLAAGntvvikpssttslsllelakiiqdvLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK-K 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 167 LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQ 246
Cdd:cd07117 238 LIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 247 GPQIDQKQFDKILELIESGKKEGAKLECGG----SAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVI 322
Cdd:cd07117 318 GAQVNKDQLDKILSYVDIAKEEGAKILTGGhrltENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658310017 323 KRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 400
Cdd:cd07117 398 DMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
35-394 |
1.47e-115 |
|
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: 345.26 E-value: 1.47e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 35 FINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATL 114
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGE---WAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 115 A------------------------------------------------------------------------------- 115
Cdd:TIGR01804 78 Akletldtgktlqetivadmdsgadvfeffaglapalngeiiplggpsfaytireplgvcvgigawnyplqiaswkiapa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 ----------------------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASrSNL 167
Cdd:TIGR01804 158 laagnamvfkpsentpltalkvaeimeeAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 168 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQG 247
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 248 PQIDQKQFDKILELIESGKKEGAKLECGGSAME----DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIK 323
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPEnvglQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658310017 324 RANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVK 394
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
53-397 |
9.91e-115 |
|
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: 342.79 E-value: 9.91e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATLA----------------- 115
Cdd:cd07110 3 NPATEATIGEIPAATAEDVDAAVRAARRAFPR---WKKTTGAERAKYLRAIAEGVRERREELAeleardngkpldeaawd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 --------------------------------------------------------------------------------
Cdd:cd07110 80 vddvagcfeyyadlaeqldakaeravplpsedfkarvrrepvgvvglitpwnfpllmaawkvapalaagctvvlkpselt 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 -------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIV 182
Cdd:cd07110 160 sltelelaeiaaeAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSPIIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 183 CADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELI 262
Cdd:cd07110 239 FDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 263 ESGKKEGAKLECGGSAME--DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKN 340
Cdd:cd07110 319 ARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 658310017 341 LDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 397
Cdd:cd07110 399 AERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
35-398 |
3.24e-113 |
|
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: 339.32 E-value: 3.24e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 35 FINNEWHESKSGKKFATCNPS-TREQICEVEEGDKPDVDKAVEAAQVAFqrgSPWRRLDALSRGRLLHQLADLVERDRAT 113
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAF---PEWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 114 LA------------------------------------------------------------------------------ 115
Cdd:cd07131 79 LArlvtremgkplaegrgdvqeaidmaqyaagegrrlfgetvpselpnkdamtrrqpigvvalitpwnfpvaipswkifp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 -----------------------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSN 166
Cdd:cd07131 159 alvcgntvvfkpaedtpacalklvelfaeAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 167 lKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQ 246
Cdd:cd07131 239 -KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 247 GPQIDQKQFDKILELIESGKKEGAKLECGGSAME----DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVI 322
Cdd:cd07131 318 GPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTgggyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658310017 323 KRANSTDYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNAlYAQAPFGGFKMSGNG-RELGEYALAEYTEVKTVTI 398
Cdd:cd07131 398 EIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNapTIGA-EVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
102-398 |
5.05e-112 |
|
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: 335.45 E-value: 5.05e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 102 QLADLVErdratlAAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCI 181
Cdd:cd07150 164 KIAEIME------EAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPLI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 182 VCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILEL 261
Cdd:cd07150 237 VLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQ 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 262 IESGKKEGAKLECGGsamEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNL 341
Cdd:cd07150 317 VEDAVAKGAKLLTGG---KYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDL 393
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 658310017 342 DKALKLASALESGTVWINCYNAL-YAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07150 394 QRAFKLAERLESGMVHINDPTILdEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
35-396 |
7.19e-112 |
|
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: 335.76 E-value: 7.19e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 35 FINNEWHESKSGKKfaTCNPS-TREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRAT 113
Cdd:cd07097 4 YIDGEWVAGGDGEE--NRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA---WRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 114 LA------------------------------------------------------------------------------ 115
Cdd:cd07097 79 LArlltreegktlpeargevtragqifryyagealrlsgetlpstrpgvevettreplgvvglitpwnfpiaipawkiap 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 -----------------------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASrSN 166
Cdd:cd07097 159 alaygntvvfkpaeltpasawalveileeAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-AR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 167 LKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQ 246
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 247 GPQIDQKQFDKILELIESGKKEGAKLECGGSA--MEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKR 324
Cdd:cd07097 318 GPVVSERQLEKDLRYIEIARSEGAKLVYGGERlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658310017 325 ANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNA-LYAQAPFGGFKMSGNG-RELGEYALAEYTEVKTV 396
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
51-400 |
1.78e-111 |
|
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: 334.34 E-value: 1.78e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 51 TCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVeRDRAT----------------- 113
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE---WRATTPLERARMLRELATRL-REHAEelalidaldcgnpvsam 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 114 ----------------------------------------------------------------LAAG------------ 117
Cdd:cd07107 77 lgdvmvaaalldyfaglvtelkgetipvggrnlhytlrepygvvarivafnhplmfaaakiaapLAAGntvvvkppeqap 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 118 -------------FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSnLKRVTLELGGKNPCIVCA 184
Cdd:cd07107 157 lsalrlaelarevLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 185 DADLDLAVECAHQGVFFN-QGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIE 263
Cdd:cd07107 236 DADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 264 SGKKEGAKLECGGSAMED----KGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTK 339
Cdd:cd07107 316 SAKREGARLVTGGGRPEGpaleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTN 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658310017 340 NLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 400
Cdd:cd07107 396 DISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
34-398 |
2.16e-109 |
|
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: 329.54 E-value: 2.16e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 34 IFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGsPWRRLDALSRGRLLHQLADLVERDRAT 113
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 114 LA------------------------------------------------------------------------------ 115
Cdd:cd07139 80 LArlwtaengmpiswsrraqgpgpaallryyaalardfpfeerrpgsggghvlvrrepvgvvaaivpwnaplflaalkia 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 ------------------------------AGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRs 165
Cdd:cd07139 160 palaagctvvlkpspetpldayllaeaaeeAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 166 NLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTE 245
Cdd:cd07139 238 RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 246 QGPQIDQKQFDKILELIESGKKEGAKLECGGS--AMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIK 323
Cdd:cd07139 318 IGPLASARQRERVEGYIAKGRAEGARLVTGGGrpAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658310017 324 RANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYnALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07139 398 IANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
111-396 |
2.71e-109 |
|
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: 328.82 E-value: 2.71e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 111 RATLAAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDL 190
Cdd:cd07089 171 EIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKSANIVLDDADLAA 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 191 AVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGA 270
Cdd:cd07089 250 AAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 271 KLECGGSAME--DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLA 348
Cdd:cd07089 330 RLVTGGGRPAglDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVA 409
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 658310017 349 SALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 396
Cdd:cd07089 410 RRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
101-398 |
1.38e-108 |
|
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: 323.80 E-value: 1.38e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 101 HQLADLVErdratlAAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPC 180
Cdd:cd06534 136 LALAELLQ------EAGLPPGVVNVVPGGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 181 IVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVeyakkrpvgdpfdvkteqgpqidqkqfdkile 260
Cdd:cd06534 209 IVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYDEFVEKLV-------------------------------- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 261 liesgkkegaklecggsamedkglfikpTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKN 340
Cdd:cd06534 257 ----------------------------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRD 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 658310017 341 LDKALKLASALESGTVWINCYNALY-AQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd06534 309 LNRALRVAERLRAGTVYINDSSIGVgPEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
19-397 |
5.11e-108 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 327.07 E-value: 5.11e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 19 ALPRPIRNLevkftkiFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQR--GSPWRRLDALSR 96
Cdd:PLN02467 2 AIPVPRRQL-------FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkGKDWARTTGAVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 97 GRLLHQLADLVERDRATLA------------------------------------------------------------- 115
Cdd:PLN02467 75 AKYLRAIAAKITERKSELAkletldcgkpldeaawdmddvagcfeyyadlaealdakqkapvslpmetfkgyvlkeplgv 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 -------------------------------------------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKI 146
Cdd:PLN02467 155 vglitpwnypllmatwkvapalaagctavlkpselasvtcleladicreVGLPPGVLNVVTGLGTEAGAPLASHPGVDKI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 147 AFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRR 226
Cdd:PLN02467 235 AFTGSTATGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 227 SVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMED--KGLFIKPTVFSEVTDNMRIAKEE 304
Cdd:PLN02467 314 LVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWREE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 305 IFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGE 384
Cdd:PLN02467 394 VFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGE 473
|
490
....*....|...
gi 658310017 385 YALAEYTEVKTVT 397
Cdd:PLN02467 474 WGLENYLSVKQVT 486
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
53-398 |
1.36e-107 |
|
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: 324.19 E-value: 1.36e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGspWRRLDALSRGRLLHQLADLVERDRATLA----------------- 115
Cdd:cd07109 3 DPSTGEVFARIARGGAADVDRAVQAARRAFESG--WLRLSPAERGRLLLRIARLIREHADELArlesldtgkpltqarad 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 --------------------------------------------------------------------------------
Cdd:cd07109 81 veaaaryfeyyggaadklhgetiplgpgyfvytvrephgvtghiipwnyplqitgrsvapalaagnavvvkpaedaplta 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 ---------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADA 186
Cdd:cd07109 161 lrlaelaeeAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 187 DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVG----DPfDVkteqGPQIDQKQFDKILELI 262
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGpgleDP-DL----GPLISAKQLDRVEGFV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 263 ESGKKEGAKLECGGSAMED---KGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTK 339
Cdd:cd07109 315 ARARARGARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTR 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 340 NLDKALKLASALESGTVWINCYNALYA-QAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07109 395 DGDRALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
53-398 |
3.95e-107 |
|
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: 323.12 E-value: 3.95e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERD---------------------- 110
Cdd:cd07092 3 DPATGEEIATVPDASAADVDAAVAAAHAAFPS---WRRTTPAERSKALLKLADAIEENaeelaalesrntgkplhlvrdd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 111 ----------------RAT--------------------------------------------LAAG------------- 117
Cdd:cd07092 80 elpgavdnfrffagaaRTLegpaageylpghtsmirrepigvvaqiapwnyplmmaawkiapaLAAGntvvlkpsettpl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 118 ------------FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCAD 185
Cdd:cd07092 160 ttlllaelaaevLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD-TLKRVHLELGGKAPVIVFDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 186 ADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIEsG 265
Cdd:cd07092 239 ADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE-R 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 266 KKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKAL 345
Cdd:cd07092 318 APAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAM 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 658310017 346 KLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07092 398 RLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
53-398 |
6.36e-105 |
|
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: 317.38 E-value: 6.36e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFQrgsPWRRLDALSRGRLLHQLADLVE------------------------ 108
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEarseelarllaletgnalrtqarp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 109 -----------------------------------RD----------------------RATLAAG-------------- 117
Cdd:cd07108 80 eaavladlfryfgglagelkgetlpfgpdvltytvREplgvvgailpwnaplmlaalkiAPALVAGntvvlkaaedapla 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 118 -----------FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLV-KEAASRsnLKRVTLELGGKNPCIVCAD 185
Cdd:cd07108 160 vlllaeilaqvLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIyRAAADR--LIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 186 ADLDLAVECAHQGV-FFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIES 264
Cdd:cd07108 238 ADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 265 GKKE-GAKLECGGSAMED----KGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTK 339
Cdd:cd07108 318 GLSTsGATVLRGGPLPGEgplaDGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 340 NLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELG-EYALAEYTEVKTVTI 398
Cdd:cd07108 398 DLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
31-401 |
2.14e-104 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 316.85 E-value: 2.14e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 31 FTKIFINNEWhESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERD 110
Cdd:PRK13473 2 QTKLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE---WSQTTPKERAEALLKLADAIEEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 111 ----------------RAT------------------------------------------------------------- 113
Cdd:PRK13473 78 adefarleslncgkplHLAlndeipaivdvfrffagaarclegkaageyleghtsmirrdpvgvvasiapwnyplmmaaw 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 114 -----LAAG-------------------------FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAAS 163
Cdd:PRK13473 158 klapaLAAGntvvlkpseitpltalklaelaadiLPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 164 RSnLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVK 243
Cdd:PRK13473 238 DS-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 244 TEQGPQIDQKQFDKILELIESGKKEG-AKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVI 322
Cdd:PRK13473 317 TELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658310017 323 KRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLG 401
Cdd:PRK13473 397 RWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVKHT 475
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
116-398 |
1.08e-100 |
|
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: 306.44 E-value: 1.08e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASrsnLKRVTLELGGKNPCIVCADADLDLAVECA 195
Cdd:cd07149 176 AGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGSNAAVIVDADADLEKAVERC 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 196 HQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECG 275
Cdd:cd07149 253 VSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVEEAVEGGARLLTG 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 276 GSAMedkGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGT 355
Cdd:cd07149 333 GKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGG 409
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 658310017 356 VWIN-CYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07149 410 VMINdSSTFRVDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
15-396 |
1.52e-100 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 307.77 E-value: 1.52e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 15 RKPPALPRPIRNLEVKFTKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQrgsPWRRLDAL 94
Cdd:PLN02278 8 MDAQSALVKLRNAGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLTAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 95 SRGRLLHQLADLVE---------------------------------------------------RDR------------ 111
Cdd:PLN02278 85 ERSKILRRWYDLIIankedlaqlmtleqgkplkeaigevaygasfleyfaeeakrvygdiipspfPDRrllvlkqpvgvv 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 112 ------------------------------------------ATLA--AGFPPGVVNIVPGFGPTVGAAISSHPQINKIA 147
Cdd:PLN02278 165 gaitpwnfplamitrkvgpalaagctvvvkpseltpltalaaAELAlqAGIPPGVLNVVMGDAPEIGDALLASPKVRKIT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 148 FTGSTEVGKLVKEAASRSnLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRS 227
Cdd:PLN02278 245 FTGSTAVGKKLMAGAAAT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 228 VEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFG 307
Cdd:PLN02278 324 SKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 308 PVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYAL 387
Cdd:PLN02278 404 PVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGI 483
|
....*....
gi 658310017 388 AEYTEVKTV 396
Cdd:PLN02278 484 DEYLEIKYV 492
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
103-399 |
1.47e-99 |
|
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: 304.23 E-value: 1.47e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 103 LADLVErdratlAAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIV 182
Cdd:cd07151 177 LAKIFE------EAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR-HLKKVALELGGNNPFVV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 183 CADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELI 262
Cdd:cd07151 250 LEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKI 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 263 ESGKKEGAKLECGGSAmedKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLD 342
Cdd:cd07151 330 EQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLE 406
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 658310017 343 KALKLASALESGTVWIN--CYNALyAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 399
Cdd:cd07151 407 RGVQFARRIDAGMTHINdqPVNDE-PHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
34-397 |
3.06e-99 |
|
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: 304.92 E-value: 3.06e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 34 IFINNEwhESKSGKKFATCNPS-TREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRA 112
Cdd:cd07124 35 LVIGGK--EVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPT---WRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 113 TLAA---------------------------------------------------------------------------- 116
Cdd:cd07124 110 ELAAwmvlevgknwaeadadvaeaidfleyyaremlrlrgfpvemvpgednryvyrplgvgavispwnfplailagmtta 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 117 ------------------------------GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASR-- 164
Cdd:cd07124 190 alvtgntvvlkpaedtpviaaklveileeaGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKvq 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 165 ---SNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFD 241
Cdd:cd07124 270 pgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPED 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 242 VKTEQGPQIDQKQFDKILELIESGKKEGaKLECGGSAMED--KGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIE 319
Cdd:cd07124 350 PEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 320 EVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWIN--CYNALYAQAPFGGFKMSG-NGRELGEYALAEYTEVKTV 396
Cdd:cd07124 429 EALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGtGSKAGGPDYLLQFMQPKTV 508
|
.
gi 658310017 397 T 397
Cdd:cd07124 509 T 509
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
115-398 |
9.63e-99 |
|
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: 301.13 E-value: 9.63e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 115 AAGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVEC 194
Cdd:cd07152 163 EAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDADLDLAASN 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 195 AHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLEC 274
Cdd:cd07152 241 GAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 275 GGSAmedKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESG 354
Cdd:cd07152 321 GGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTG 397
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 658310017 355 TVWINCYNALY-AQAPFGGFKMSGNGRELGEYA-LAEYTEVKTVTI 398
Cdd:cd07152 398 MLHINDQTVNDePHNPFGGMGASGNGSRFGGPAnWEEFTQWQWVTV 443
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
103-398 |
2.34e-98 |
|
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: 300.80 E-value: 2.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 103 LADLVERdratlaAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLV-KEAASRsnLKRVTLELGGKNPCI 181
Cdd:cd07145 169 LAKILEE------AGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIaSKAGGT--GKKVALELGGSDPMI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 182 VCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILEL 261
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENL 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 262 IESGKKEGAKLECGGSAMEdkGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNL 341
Cdd:cd07145 321 VNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDI 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 658310017 342 DKALKLASALESGTVWINCYNAL-YAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07145 399 NRALKVARELEAGGVVINDSTRFrWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
35-398 |
2.38e-98 |
|
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: 301.40 E-value: 2.38e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 35 FINNEWHESkSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATL 114
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE---WRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 115 AA------------------------------------------------------------------------------ 116
Cdd:cd07086 78 GRlvslemgkilpeglgevqemidicdyavglsrmlygltipserpghrlmeqwnplgvvgvitafnfpvavpgwnaaia 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 117 ---------------------------------GFPPGVVNIVPGFGPtVGAAISSHPQINKIAFTGSTEVGKLVKEAAS 163
Cdd:cd07086 158 lvcgntvvwkpsettpltaiavtkilaevleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 164 RSNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVK 243
Cdd:cd07086 237 RRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 244 TEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAME--DKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEV 321
Cdd:cd07086 316 TLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDggEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 322 IKRANSTDYGLTAAVFTKNLDKALKLASALES--GTVWIN--CYNAlYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 397
Cdd:cd07086 396 IAINNDVPQGLSSSIFTEDLREAFRWLGPKGSdcGIVNVNipTSGA-EIGGAFGGEKETGGGRESGSDAWKQYMRRSTCT 474
|
.
gi 658310017 398 I 398
Cdd:cd07086 475 I 475
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
35-390 |
6.18e-98 |
|
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: 300.47 E-value: 6.18e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 35 FINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVE------ 108
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES---WSALPGHVRARHLYRIARHIQkhqrlf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 109 ---------------RDR-------------------------------------------------------------- 111
Cdd:cd07111 102 avlesldngkpiresRDCdiplvarhfyhhagwaqlldtelagwkpvgvvgqivpwnfpllmlawkicpalamgntvvlk 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 112 ------------ATLA--AGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSNlKRVTLELGGK 177
Cdd:cd07111 182 paeytpltallfAEICaeAGLPPGVLNIVTG-NGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTG-KKLSLELGGK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 178 NPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDK 257
Cdd:cd07111 260 SPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 258 ILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVF 337
Cdd:cd07111 340 IRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVW 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 658310017 338 TKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEY 390
Cdd:cd07111 420 SENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
114-398 |
3.20e-97 |
|
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: 296.68 E-value: 3.20e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 114 LAAGFPPGVVNIVPGFGPTVGAAISsHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVE 193
Cdd:cd07100 147 REAGFPEGVFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 194 CAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLE 273
Cdd:cd07100 225 TAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 274 CGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALES 353
Cdd:cd07100 305 LGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEA 384
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 658310017 354 GTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07100 385 GMVFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
111-398 |
7.89e-93 |
|
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: 285.63 E-value: 7.89e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 111 RATLAAGFPPGVVNIV---PGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADAD 187
Cdd:cd07105 146 RVFHEAGLPKGVLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDAD 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 188 LDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDpfdvkTEQGPQIDQKQFDKILELIESGKK 267
Cdd:cd07105 225 LDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 268 EGAKLECGG-SAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALK 346
Cdd:cd07105 300 KGAKLVVGGlADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALA 379
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 658310017 347 LASALESGTVWINCYNaLY--AQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07105 380 VAKRIESGAVHINGMT-VHdePTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
90-399 |
2.46e-90 |
|
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: 280.61 E-value: 2.46e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 90 RLDALSRGRLLHQLADlverdratlaAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsnlKR 169
Cdd:cd07082 178 TQGVLLGIPLAEAFHD----------AGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPM---KR 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 170 VTLELGGKNPCIVCADADLDLAV-ECAHQGVFFNqGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGP 248
Cdd:cd07082 245 LVLELGGKDPAIVLPDADLELAAkEIVKGALSYS-GQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITP 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 249 QIDQKQFDKILELIESGKKEGAKLECGGSAMEdkGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANST 328
Cdd:cd07082 324 LIDPKSADFVEGLIDDAVAKGATVLNGGGREG--GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKS 401
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658310017 329 DYGLTAAVFTKNLDKALKLASALESGTVWINCYNA----LYaqaPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 399
Cdd:cd07082 402 NYGLQASIFTKDINKARKLADALEVGTVNINSKCQrgpdHF---PFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
35-399 |
1.33e-89 |
|
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: 278.94 E-value: 1.33e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 35 FINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQrgSPWRRLDALSRGRLLHQLADLVERDRATL 114
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 115 A------------------------------------------------------------------------------- 115
Cdd:cd07113 81 Aqletlcsgksihlsrafevgqsanflryfagwatkingetlapsipsmqgerytaftrrepvgvvagivpwnfsvmiav 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 ----------------------------------AGFPPGVVNIVPGFGpTVGAAISSHPQINKIAFTGSTEVGKLVKEA 161
Cdd:cd07113 161 wkigaalatgctivikpseftpltllrvaelakeAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 162 ASrSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFD 241
Cdd:cd07113 240 AA-SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 242 VKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEV 321
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658310017 322 IKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 399
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
116-400 |
3.06e-89 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 279.13 E-value: 3.06e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSN-----LKRVTLELGGKNPCIVCADADLDL 190
Cdd:PRK03137 224 AGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQpgqiwLKRVIAEMGGKDAIVVDEDADLDL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 191 AVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDvKTEQGPQIDQKQFDKILELIESGKKEGa 270
Cdd:PRK03137 304 AAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPED-NAYMGPVINQASFDKIMSYIEIGKEEG- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 271 KLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASA 350
Cdd:PRK03137 382 RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARRE 461
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 658310017 351 LESGTVWIN--CYNALYAQAPFGGFKMSGNGRELG--EYaLAEYTEVKTVTIKL 400
Cdd:PRK03137 462 FHVGNLYFNrgCTGAIVGYHPFGGFNMSGTDSKAGgpDY-LLLFLQAKTVSEMF 514
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
115-398 |
1.42e-87 |
|
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: 272.94 E-value: 1.42e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 115 AAGFPPGVVNIVPGFGPTvGAAISSHPqINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVEC 194
Cdd:cd07099 171 AAGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPMIVLADADLERAAAA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 195 AHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLEC 274
Cdd:cd07099 248 AVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALT 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 275 GGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESG 354
Cdd:cd07099 328 GGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAG 407
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 658310017 355 TVWINC--YNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07099 408 AVSINDvlLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
32-400 |
2.39e-87 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 273.70 E-value: 2.39e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 32 TKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGSpWRRLDALSRGRLLHQLADLVERDR 111
Cdd:PRK09847 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLADLMEAHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 112 ATLA---------------------------------------------------------------------------- 115
Cdd:PRK09847 99 EELAlletldtgkpirhslrddipgaarairwyaeaidkvygevattsshelamivrepvgviaaivpwnfpllltcwkl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 -------------------------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASR 164
Cdd:PRK09847 179 gpalaagnsvilkpseksplsairlaglakeAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 165 SNLKRVTLELGGKNPCIVCADA-DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVK 243
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 244 TEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDkgLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIK 323
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLA--AAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658310017 324 RANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 400
Cdd:PRK09847 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISL 493
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
53-397 |
2.83e-85 |
|
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: 266.90 E-value: 2.83e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 53 NPSTREQICEVEEGDKPDVDKAVEAAQVAFqRGSPWRRlDALSRGRLLHQLADLVERDR--------------------- 111
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAF-DETDWAH-DPRLRARVLLELADAFEANAerlarllalengkilgearfe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 112 -----------------------------------------------------------ATLAAG--------------- 117
Cdd:cd07120 81 isgaiselryyaglarteagrmiepepgsfslvlrepmgvagiivpwnspvvllvrslaPALAAGctvvvkpagqtaqin 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 118 ------------FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASrSNLKRVTLELGGKNPCIVCAD 185
Cdd:cd07120 161 aaiirilaeipsLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTPCIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 186 ADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESG 265
Cdd:cd07120 240 ADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 266 KKEGAK-LECGGSAMED--KGLFIKPTVFsEVTDN-MRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNL 341
Cdd:cd07120 320 IAAGAEvVLRGGPVTEGlaKGAFLRPTLL-EVDDPdADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 658310017 342 DKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 397
Cdd:cd07120 399 ARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
103-398 |
3.61e-84 |
|
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: 263.91 E-value: 3.61e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 103 LADLVERdratlaAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASrsnLKRVTLELGGKNPCIV 182
Cdd:cd07094 169 LAKILVE------AGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNAPVIV 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 183 CADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELI 262
Cdd:cd07094 240 DRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWV 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 263 ESGKKEGAKLECGGsamEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLD 342
Cdd:cd07094 320 EEAVEAGARLLCGG---ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLN 396
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 658310017 343 KALKLASALESGTVWINCYNALYAQA-PFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07094 397 VAFKAAEKLEVGGVMVNDSSAFRTDWmPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
116-397 |
4.14e-84 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 265.97 E-value: 4.14e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 AGFPPGVVNIVPGFGPTVGAAISSHpqINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECA 195
Cdd:PRK09407 207 AGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGR-RLIGFSLELGGKNPMIVLDDADLDKAAAGA 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 196 HQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECG 275
Cdd:PRK09407 284 VRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAG 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 276 GSAMEDKG-LFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESG 354
Cdd:PRK09407 364 GKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAG 443
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 658310017 355 TVWIN-CYNALYA--QAPFGGFKMSGNGRELGEYALAEYTEVKTVT 397
Cdd:PRK09407 444 TVNVNeGYAAAWGsvDAPMGGMKDSGLGRRHGAEGLLKYTESQTIA 489
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
111-397 |
3.62e-83 |
|
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: 261.47 E-value: 3.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 111 RATLAAGFPPGVVNIVPGFGPTVGAAISSHpqINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDL 190
Cdd:cd07101 166 ELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGR-RLIGCSLELGGKNPMIVLEDADLDK 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 191 AVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGA 270
Cdd:cd07101 243 AAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 271 KLECGGSAMEDKG-LFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLAS 349
Cdd:cd07101 323 TVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAA 402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 658310017 350 ALESGTVWIN-CYNALYA--QAPFGGFKMSGNGRELGEYALAEYTEVKTVT 397
Cdd:cd07101 403 RLRAGTVNVNeGYAAAWAsiDAPMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
35-398 |
2.78e-82 |
|
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: 260.08 E-value: 2.78e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 35 FINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERD---- 110
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA---WGKTSVAERANILNKIADRMEANleml 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 111 ----------------------------------RA-------------------------------------------T 113
Cdd:cd07116 81 avaetwdngkpvretlaadiplaidhfryfagciRAqegsiseidentvayhfheplgvvgqiipwnfpllmatwklapA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 114 LAAG-------------------------FPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLK 168
Cdd:cd07116 161 LAAGncvvlkpaeqtpasilvlmeligdlLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 169 RVTLELGGKNPCIVCA------DADLDLAVECAhqGVF-FNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFD 241
Cdd:cd07116 240 PVTLELGGKSPNIFFAdvmdadDAFFDKALEGF--VMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 242 VKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGL----FIKPTVFSEvTDNMRIAKEEIFGPVQPILKFKS 317
Cdd:cd07116 318 TETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 318 IEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 397
Cdd:cd07116 397 EEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLL 476
|
.
gi 658310017 398 I 398
Cdd:cd07116 477 V 477
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
111-397 |
6.39e-82 |
|
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: 258.77 E-value: 6.39e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 111 RATLAA-GFPPGVVNIVPGFGPTvGAAISSHPQINKIAFTGSTEVGKLVKEAASRSnLKRVTLELGGKNPCIVCADADLD 189
Cdd:cd07098 171 RECLAAcGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LTPVVLELGGKDPAIVLDDADLD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 190 LAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEG 269
Cdd:cd07098 249 QIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKG 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 270 AKLECGGS----AMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKAL 345
Cdd:cd07098 329 ARLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRAR 408
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 658310017 346 KLASALESGTVWINCYNALY--AQAPFGGFKMSGNGRELGEYALAEYTEVKTVT 397
Cdd:cd07098 409 RIASQLETGMVAINDFGVNYyvQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
115-399 |
1.19e-81 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 256.20 E-value: 1.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 115 AAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVEC 194
Cdd:PRK10090 123 EIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDLAVKA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 195 AHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFD-VKTEQGPQIDQKQFDKILELIESGKKEGAKLE 273
Cdd:PRK10090 202 IVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 274 CGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALES 353
Cdd:PRK10090 282 LGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKF 361
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 658310017 354 GTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 399
Cdd:PRK10090 362 GETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQTQVVYLQ 407
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
103-398 |
2.19e-79 |
|
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: 251.51 E-value: 2.19e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 103 LADLVERdratlaAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASrsnLKRVTLELGGKNPCIV 182
Cdd:cd07146 166 LADLLYE------AGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGNDPLIV 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 183 CADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELI 262
Cdd:cd07146 237 MDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRV 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 263 ESGKKEGAKLECGGsamEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLD 342
Cdd:cd07146 317 EEAIAQGARVLLGN---QRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLD 393
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 658310017 343 KALKLASALESGTVWINCYNALYAQ-APFGGFKMSGNG-RELGEYALAEYTEVKTVTI 398
Cdd:cd07146 394 TIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
115-396 |
3.77e-76 |
|
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: 243.31 E-value: 3.77e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 115 AAGFPPGVVNIVPGFGPTvGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVEC 194
Cdd:cd07102 168 EAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAYVRPDADLDAAAES 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 195 AHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLEC 274
Cdd:cd07102 246 LVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALI 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 275 GG---SAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASAL 351
Cdd:cd07102 326 DGalfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQL 405
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 658310017 352 ESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 396
Cdd:cd07102 406 ETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
32-397 |
1.72e-72 |
|
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: 234.33 E-value: 1.72e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 32 TKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDR 111
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA---WSATPVLKRQQVMFKFRQLLEENL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 112 ATLA---------------------------------------------------------------------------- 115
Cdd:cd07085 78 DELArlitlehgktladargdvlrglevvefacsiphllkgeylenvargidtysyrqplgvvagitpfnfpamiplwmf 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 -------------------------------AGFPPGVVNIVPGFGPTVGAaISSHPQINKIAFTGSTEVGKLVKEAASR 164
Cdd:cd07085 158 pmaiacgntfvlkpservpgaamrlaellqeAGLPDGVLNVVHGGKEAVNA-LLDHPDIKAVSFVGSTPVGEYIYERAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 165 SNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKT 244
Cdd:cd07085 237 NG-KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 245 EQGPQIDQKQFDKILELIESGKKEGAKLECGG----SAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEE 320
Cdd:cd07085 316 DMGPVISPAAKERIEGLIESGVEEGAKLVLDGrgvkVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 321 VIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNAL-YAQAPFGGFKMS--GNGRELGEYALAEYTEVKTVT 397
Cdd:cd07085 396 AIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVpLAFFSFGGWKGSffGDLHFYGKDGVRFYTQTKTVT 475
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
103-400 |
3.26e-72 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 234.03 E-value: 3.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 103 LADLVERdratlaAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIV 182
Cdd:PRK11241 192 LAELAIR------AGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK-DIKKVSLELGGNAPFIV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 183 CADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELI 262
Cdd:PRK11241 265 FDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHI 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 263 ESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLD 342
Cdd:PRK11241 345 ADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLS 424
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 658310017 343 KALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 400
Cdd:PRK11241 425 RVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
114-398 |
8.37e-72 |
|
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: 232.14 E-value: 8.37e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 114 LAAGFPPGVVNIVPGfgPTVGAAI-SSHPQINKIAFTGSTEVGKLVKEAASRsnlKRVTLELGGKNPCIVCADADLDLAV 192
Cdd:cd07147 174 AETGLPKGAFSVLPC--SRDDADLlVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGNAAVIVDSDADLDFAA 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 193 ECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKL 272
Cdd:cd07147 249 QRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVDAGAKL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 273 ECGGsamEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALE 352
Cdd:cd07147 329 LTGG---KRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELE 405
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 658310017 353 SGTVWINCYNALYA-QAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07147 406 VGGVVINDVPTFRVdHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
116-397 |
2.30e-64 |
|
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: 213.98 E-value: 2.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASR-----SNLKRVTLELGGKNPCIVCADADLDL 190
Cdd:cd07083 207 AGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARlapgqTWFKRLYVETGGKNAIIVDETADFEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 191 AVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGa 270
Cdd:cd07083 287 VVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 271 KLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIE--EVIKRANSTDYGLTAAVFTKNLDKALKLA 348
Cdd:cd07083 366 QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEAR 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 658310017 349 SALESGTVWIN--CYNALYAQAPFGGFKMSG-NGRELGEYALAEYTEVKTVT 397
Cdd:cd07083 446 REFHVGNLYINrkITGALVGVQPFGGFKLSGtNAKTGGPHYLRRFLEMKAVA 497
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
115-396 |
8.07e-63 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 208.95 E-value: 8.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 115 AAGFPPGVVNIVPGFGPTVGAAISShPQINKIAFTGSTEVGKLVKEAASRSnLKRVTLELGGKNPCIVCADADLDLAVEC 194
Cdd:PRK13968 178 DAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGGSDPFIVLNDADLELAVKA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 195 AHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLEC 274
Cdd:PRK13968 256 AVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGARLLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 275 GGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESG 354
Cdd:PRK13968 336 GGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECG 415
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 658310017 355 TVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 396
Cdd:PRK13968 416 GVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
103-398 |
4.67e-61 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 204.20 E-value: 4.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 103 LADLVERdratlaAGFPPGVVNIVpgfgpTVGA----AISSHPQINKIAFTGSTEVGKLVKEAASRSnLKRVTLELGGKN 178
Cdd:PRK09406 169 LADLFRR------AGFPDGCFQTL-----LVGSgaveAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVLELGGSD 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 179 PCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKI 258
Cdd:PRK09406 237 PFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEV 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 259 LELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFT 338
Cdd:PRK09406 317 EKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWT 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 339 KNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:PRK09406 397 RDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
111-401 |
1.58e-59 |
|
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: 200.51 E-value: 1.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 111 RATLAAGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDL 190
Cdd:cd07130 184 RVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAA-RFGRSLLELGGNNAIIVMEDADLDL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 191 AVecahQGVFF----NQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGK 266
Cdd:cd07130 262 AV----RAVLFaavgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAK 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 267 KEGAKLECGGSAMEDKGLFIKPTVFsEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALK 346
Cdd:cd07130 338 SQGGTVLFGGKVIDGPGNYVEPTIV-EGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFR 416
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 658310017 347 LASALESGTVWINCyNALYAQA----PFGGFKMSGNGRELGEYALAEYTEVKTVTIKLG 401
Cdd:cd07130 417 WLGPKGSDCGIVNV-NIGTSGAeiggAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
118-398 |
2.96e-57 |
|
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: 193.13 E-value: 2.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 118 FPPGVVNIVPGfGPTVGAAISSHPqINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQ 197
Cdd:cd07087 154 FDPEAVAVVEG-GVEVATALLAEP-FDHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIAW 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 198 GVFFNQGQCCTAASRVFVEEQVYSEFVrrsvEYAKKRpvgdpfdVKTEQGPQ----------IDQKQFDKILELIESGKk 267
Cdd:cd07087 231 GKFLNAGQTCIAPDYVLVHESIKDELI----EELKKA-------IKEFYGEDpkespdygriINERHFDRLASLLDDGK- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 268 egakLECGGSAmEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKL 347
Cdd:cd07087 299 ----VVIGGQV-DKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERV 373
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 658310017 348 ASALESGTVwinCYNALYAQA-----PFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07087 374 LAETSSGGV---CVNDVLLHAaipnlPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
118-396 |
6.12e-57 |
|
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: 192.83 E-value: 6.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 118 FPPGVVNIVPGfGPTVGAAISSHPqINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQ 197
Cdd:cd07134 154 FDEDEVAVFEG-DAEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAW 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 198 GVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQI-DQKQFDKILELIESGKKEGAKLECGG 276
Cdd:cd07134 231 GKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASPDLARIvNDRHFDRLKGLLDDAVAKGAKVEFGG 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 277 sAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTV 356
Cdd:cd07134 311 -QFDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGV 389
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 658310017 357 WIN--CYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 396
Cdd:cd07134 390 VVNdvVLHFLNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
118-385 |
1.48e-55 |
|
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: 189.25 E-value: 1.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 118 FPPGVVNIVPGfGPTVGAAISSHPqINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQ 197
Cdd:cd07136 154 FDEEYVAVVEG-GVEENQELLDQK-FDYIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKRIVW 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 198 GVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKtEQGPQIDQKQFDKILELIESGKkegakLECGGS 277
Cdd:cd07136 231 GKFLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLLDNGK-----IVFGGN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 278 AmEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVW 357
Cdd:cd07136 305 T-DRETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGC 383
|
250 260 270
....*....|....*....|....*....|..
gi 658310017 358 INcyNALYAQA----PFGGFKMSGNGRELGEY 385
Cdd:cd07136 384 IN--DTIMHLAnpylPFGGVGNSGMGSYHGKY 413
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
33-400 |
1.35e-53 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 185.34 E-value: 1.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 33 KIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAfQRGspWRRLDALSRGRLLHQLA-------- 104
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA-QKA--WAKTPLWKRAELLHKAAailkehka 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 105 -------------------------DLV-------------------------ERDRATLA------------------- 115
Cdd:PLN00412 94 piaeclvkeiakpakdavtevvrsgDLIsytaeegvrilgegkflvsdsfpgnERNKYCLTskiplgvvlaippfnypvn 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 -------------------------------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGStEVGKLV 158
Cdd:PLN00412 174 lavskiapaliagnavvlkpptqgavaalhmvhcfhlAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 159 KEAASRSNLKrvtLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGD 238
Cdd:PLN00412 253 SKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 239 PFDvKTEQGPQIDQKQFDKILELIESGKKEGAKLEcggSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSI 318
Cdd:PLN00412 330 PED-DCDITPVVSESSANFIEGLVMDAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 319 EEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYA-QAPFGGFKMSGNGRELGEYALAEYTEVKTVT 397
Cdd:PLN00412 406 EEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIGSQGITNSINMMTKVKSTV 485
|
...
gi 658310017 398 IKL 400
Cdd:PLN00412 486 INL 488
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
114-377 |
2.20e-52 |
|
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: 182.79 E-value: 2.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 114 LAAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGK-LVKEAASR----SNLKRVTLELGGKNPCIVCADADL 188
Cdd:cd07123 220 EEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKsLWKQIGENldryRTYPRIVGETGGKNFHLVHPSADV 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 189 DLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKE 268
Cdd:cd07123 300 DSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSD 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 269 -GAKLECGGSAMEDKGLFIKPTVFsEVTD-NMRIAKEEIFGPVQPIL-----KFKSIEEVIKraNSTDYGLTAAVFTKNl 341
Cdd:cd07123 380 pEAEIIAGGKCDDSVGYFVEPTVI-ETTDpKHKLMTEEIFGPVLTVYvypdsDFEETLELVD--TTSPYALTGAIFAQD- 455
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 658310017 342 DKALKLAS-ALE--SGTVWIN--CYNALYAQAPFGGFKMSG 377
Cdd:cd07123 456 RKAIREATdALRnaAGNFYINdkPTGAVVGQQPFGGARASG 496
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
115-391 |
7.49e-52 |
|
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: 179.00 E-value: 7.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 115 AAGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVEC 194
Cdd:cd07095 149 EAGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 195 AHQGVFFNQGQCCTAASRVFVEE-QVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLE 273
Cdd:cd07095 228 IVQSAFLTAGQRCTCARRLIVPDgAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 274 CGGSAMEDKGLFIKPTVFsEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALES 353
Cdd:cd07095 308 LAMERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRA 386
|
250 260 270
....*....|....*....|....*....|....*....
gi 658310017 354 GTV-WINCYNALYAQAPFGGFKMSGNGRELGEYAlAEYT 391
Cdd:cd07095 387 GIVnWNRPTTGASSTAPFGGVGLSGNHRPSAYYA-ADYC 424
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
111-396 |
1.37e-51 |
|
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: 178.45 E-value: 1.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 111 RATLAAGFPPGVVNIVPGfGPTVGAAISSHPqINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDL 190
Cdd:cd07133 148 AELLAEYFDEDEVAVVTG-GADVAAAFSSLP-FDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 191 AVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKR-PvgdpfDVKTeqGPQ----IDQKQFDKILELIESG 265
Cdd:cd07133 225 AAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyP-----TLAD--NPDytsiINERHYARLQGLLEDA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 266 KKEGAKL-ECGGSAMEDKGL-FIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDK 343
Cdd:cd07133 298 RAKGARViELNPAGEDFAATrKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAE 377
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 658310017 344 ALKLASALESGTVWINcyNALY--AQ--APFGGFKMSGNGRELGEYALAEYTEVKTV 396
Cdd:cd07133 378 QDRVLRRTHSGGVTIN--DTLLhvAQddLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
116-398 |
4.34e-51 |
|
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: 177.61 E-value: 4.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 AGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVkeaasRSNLK---RVTLELGGKNPCIVCADADLDLAV 192
Cdd:cd07148 177 AGLPEGWCQAVPC-ENAVAEKLVTDPRVAFFSFIGSARVGWML-----RSKLApgtRCALEHGGAAPVIVDRSADLDAMI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 193 ECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKL 272
Cdd:cd07148 251 PPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 273 ECGGSAMEDKGLfiKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALE 352
Cdd:cd07148 331 LCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLD 408
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 658310017 353 SGTVWINCYNALYAQ-APFGGFKMSGNGRELGEYALAEYTEVKTVTI 398
Cdd:cd07148 409 ATAVMVNDHTAFRVDwMPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI 455
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
103-396 |
2.05e-49 |
|
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: 172.79 E-value: 2.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 103 LADLVERdratlaaGFPPGVVNIVPGFGPTVGAAISSHpqINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIV 182
Cdd:cd07135 154 LAELVPK-------YLDPDAFQVVQGGVPETTALLEQK--FDKIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 183 CADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDvKTEQGPQIDQKQFDKILELI 262
Cdd:cd07135 224 TKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANA-SPDYTRIVNPRHFNRLKSLL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 263 ESGKkegAKLECGGSaMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKnlD 342
Cdd:cd07135 303 DTTK---GKVVIGGE-MDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTD--D 376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 658310017 343 KALK---LASALESGTVWINCY-NALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTV 396
Cdd:cd07135 377 KSEIdhiLTRTRSGGVVINDTLiHVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
35-398 |
8.18e-49 |
|
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: 173.15 E-value: 8.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 35 FINNEWHESKSGKkfATCNPS-TREQICEVEEGDKPDVDKAVEAAQVAFqrgSPWRRLDALSRGRLLHQLADLVERDRA- 112
Cdd:cd07125 36 IINGEETETGEGA--PVIDPAdHERTIGEVSLADAEDVDAALAIAAAAF---AGWSATPVEERAEILEKAADLLEANRGe 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 113 -----------TLA------------------------------------------------------------------ 115
Cdd:cd07125 111 lialaaaeagkTLAdadaevreaidfcryyaaqarelfsdpelpgptgelnglelhgrgvfvcispwnfplaiftgqiaa 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 -----------------------------AGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSN 166
Cdd:cd07125 191 alaagntviakpaeqtpliaaravellheAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 167 LKRVTL--ELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKT 244
Cdd:cd07125 271 GPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLST 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 245 EQGPQIDQKQFDKILELIESGKKEgAKLECGGSAMEDKGLFIKPTVFSEVTDNMRiaKEEIFGPVQPILKFKS--IEEVI 322
Cdd:cd07125 351 DVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVGIFDL--TTEVFGPILHVIRFKAedLDEAI 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 323 KRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINcYN---ALYAQAPFGGFKMSGNGRELG--EYaLAEYTEVKTVT 397
Cdd:cd07125 428 EDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN-RNitgAIVGRQPFGGWGLSGTGPKAGgpNY-LLRFGNEKTVS 505
|
.
gi 658310017 398 I 398
Cdd:cd07125 506 L 506
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
84-405 |
5.05e-44 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 160.00 E-value: 5.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 84 RGSPWRRLDALSRGRLLhqlADLVERDratlaaGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAAS 163
Cdd:PLN02315 188 KGAPTTPLITIAMTKLV---AEVLEKN------NLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 164 rSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVK 243
Cdd:PLN02315 258 -ARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 244 TEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFsEVTDNMRIAKEEIFGPVQPILKFKSIEEVIK 323
Cdd:PLN02315 337 TLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 324 RANSTDYGLTAAVFTKNLDKALKLASALES--GTVWINC-YNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKL 400
Cdd:PLN02315 416 INNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTINY 495
|
....*
gi 658310017 401 GDKNP 405
Cdd:PLN02315 496 GNELP 500
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
118-399 |
7.10e-44 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 159.42 E-value: 7.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 118 FPPGVVNIVPGfGPTVGAAISSHPqINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQ 197
Cdd:PTZ00381 163 LDPSYVRVIEG-GVEVTTELLKEP-FDHIFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAW 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 198 GVFFNQGQCCTAASRVFVEEQVYSEFVrRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESgkkEGAKLECGGS 277
Cdd:PTZ00381 240 GKFLNAGQTCVAPDYVLVHRSIKDKFI-EALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 278 AMEDKgLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVW 357
Cdd:PTZ00381 316 VDIEN-KYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVV 394
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 658310017 358 IN--CYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIK 399
Cdd:PTZ00381 395 INdcVFHLLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
145-399 |
1.15e-40 |
|
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: 149.68 E-value: 1.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 145 KIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFV 224
Cdd:cd07132 179 YIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFV 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 225 rrsvEYAK---KRPVGDpfDVKTEQ--GPQIDQKQFDKILELIESGKkegakLECGGSaMEDKGLFIKPTVFSEVTDNMR 299
Cdd:cd07132 258 ----EALKktlKEFYGE--DPKESPdyGRIINDRHFQRLKKLLSGGK-----VAIGGQ-TDEKERYIAPTVLTDVKPSDP 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 300 IAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVwinCYN-----ALYAQAPFGGFK 374
Cdd:cd07132 326 VMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGV---CVNdtimhYTLDSLPFGGVG 402
|
250 260
....*....|....*....|....*
gi 658310017 375 MSGNGRELGEYALAEYTEVKTVTIK 399
Cdd:cd07132 403 NSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
98-398 |
4.70e-39 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 149.19 E-value: 4.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 98 RLLHQladlverdratlaAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEA-ASRSNlKRVTL--EL 174
Cdd:PRK11904 732 KLLHE-------------AGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTlAARDG-PIVPLiaET 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 175 GGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAAsRV-FVEEQVYS---EFVRRSVEYAKkrpVGDPFDVKTEQGPQI 250
Cdd:PRK11904 798 GGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSAL-RVlFVQEDIADrviEMLKGAMAELK---VGDPRLLSTDVGPVI 873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 251 DQKQFDKILELIESGKKEG---AKLECGGSAmeDKGLFIKPTVFsEVtDNMRIAKEEIFGPVQPILKFKS--IEEVIKRA 325
Cdd:PRK11904 874 DAEAKANLDAHIERMKREArllAQLPLPAGT--ENGHFVAPTAF-EI-DSISQLEREVFGPILHVIRYKAsdLDKVIDAI 949
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658310017 326 NSTDYGLTAAVFTKNLDKALKLASALESGTVWINcYNALYA----QaPFGGFKMSGNG-RELGEYALAEYTEVKTVTI 398
Cdd:PRK11904 950 NATGYGLTLGIHSRIEETADRIADRVRVGNVYVN-RNQIGAvvgvQ-PFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1025
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
35-390 |
6.01e-38 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 142.79 E-value: 6.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 35 FINNEWHESkSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFqrgSPWRRLDALSRGRLLHQLADLVERDRATL 114
Cdd:PRK09457 4 WINGDWIAG-QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF---PAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 115 A------------------------------------------------------------------------------- 115
Cdd:PRK09457 80 Aeviaretgkplweaatevtaminkiaisiqayhertgekrsemadgaavlrhrphgvvavfgpynfpghlpnghivpal 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 ---------------------------AGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVGKLV-KEAASRSNl 167
Cdd:PRK09457 160 lagntvvfkpseltpwvaeltvklwqqAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLhRQFAGQPE- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 168 KRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSE-FVRRSVEYAKKRPVGDPFDvkTEQ 246
Cdd:PRK09457 238 KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLTVGRWDA--EPQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 247 ---GPQIDQKQFDKILE----LIESGKK---EGAKLECGGSamedkglFIKPTVFsEVTDNMRIAKEEIFGPVQPILKFK 316
Cdd:PRK09457 316 pfmGAVISEQAAQGLVAaqaqLLALGGKsllEMTQLQAGTG-------LLTPGII-DVTGVAELPDEEYFGPLLQVVRYD 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658310017 317 SIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTV-WINCYNALYAQAPFGGFKMSGNGRELGEYAlAEY 390
Cdd:PRK09457 388 DFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNHRPSAYYA-ADY 461
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
114-383 |
7.04e-37 |
|
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: 140.43 E-value: 7.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 114 LAAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTL--ELGGKNPCIVCADADLDLA 191
Cdd:TIGR01238 211 QEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIVDSTALPEQV 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 192 VECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEG-- 269
Cdd:TIGR01238 291 VRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQkk 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 270 -AKLECGGSAMEDKGLFIKPTVFSevTDNMRIAKEEIFGPVQPILKFKS--IEEVIKRANSTDYGLTAAVFTKNLDKALK 346
Cdd:TIGR01238 371 iAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVHSRIETTYRW 448
|
250 260 270
....*....|....*....|....*....|....*....
gi 658310017 347 LASALESGTVWIN--CYNALYAQAPFGGFKMSGNGRELG 383
Cdd:TIGR01238 449 IEKHARVGNCYVNrnQVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
42-379 |
7.55e-37 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 142.77 E-value: 7.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 42 ESKSGKKFATCNPS-TREQICEVEEGDKPDVDKAVEAAQVAFQRgspWRRLDALSRGRLLHQLADLVERDRATL------ 114
Cdd:COG4230 565 EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPA---WSATPVEERAAILERAADLLEAHRAELmallvr 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 --------------------------------------------------------------------------------
Cdd:COG4230 642 eagktlpdaiaevreavdfcryyaaqarrlfaaptvlrgrgvfvcispwnfplaiftgqvaaalaagntvlakpaeqtpl 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 115 ----------AAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVkeaaSRSNLKR----VTL--ELGGKN 178
Cdd:COG4230 722 iaaravrllhEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLI----NRTLAARdgpiVPLiaETGGQN 797
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 179 PCIV---------CADadldlAVECAhqgvFFNQGQCCTAAsRV-FVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGP 248
Cdd:COG4230 798 AMIVdssalpeqvVDD-----VLASA----FDSAGQRCSAL-RVlCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGP 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 249 QIDQKQFDKILELIESGKKEGAKL-ECGGSAMEDKGLFIKPTVFsEVtDNMRIAKEEIFGPVQPILKFKS--IEEVIKRA 325
Cdd:COG4230 868 VIDAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVAPTLI-EI-DSISDLEREVFGPVLHVVRYKAdeLDKVIDAI 945
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 658310017 326 NSTDYGLTAAVFTKNLDKALKLASALESGTVWINcYNALYA----QaPFGGFKMSGNG 379
Cdd:COG4230 946 NATGYGLTLGVHSRIDETIDRVAARARVGNVYVN-RNIIGAvvgvQ-PFGGEGLSGTG 1001
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
98-379 |
1.40e-35 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 139.23 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 98 RLLHQladlverdratlaAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLV-KEAASRSNlKRVTL--EL 174
Cdd:PRK11905 724 RLLHE-------------AGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIqRTLAKRSG-PPVPLiaET 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 175 GGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAAsRV-FVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQK 253
Cdd:PRK11905 790 GGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSAL-RVlCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAE 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 254 QFDKILELIESGKKEGAKL-ECGGSAMEDKGLFIKPTVFsEVtDNMRIAKEEIFGPVQPILKFKS--IEEVIKRANSTDY 330
Cdd:PRK11905 869 AQANIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLI-EI-DSISDLEREVFGPVLHVVRFKAdeLDRVIDDINATGY 946
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 658310017 331 GLTAAVFTKNLDKALKLASALESGTVWINcYNALYA----QaPFGGFKMSGNG 379
Cdd:PRK11905 947 GLTFGLHSRIDETIAHVTSRIRAGNIYVN-RNIIGAvvgvQ-PFGGEGLSGTG 997
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
112-396 |
5.96e-33 |
|
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: 128.30 E-value: 5.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 112 ATLAAGFP----PGVVNIVPGfGPTVGAAISSHpQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADAD 187
Cdd:cd07137 145 ALLAKLIPeyldTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVD 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 188 LDLAVECAHQGVF-FNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQgpQIDQKQFDKILELIESGK 266
Cdd:cd07137 222 LKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLS--RIVNSHHFQRLSRLLDDP 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 267 KEGAKLECGGSAMEDKgLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALK 346
Cdd:cd07137 300 SVADKIVHGGERDEKN-LYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRR 378
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 658310017 347 LASALESGTVWINCYNALYA--QAPFGGFKMSGNGRELGEYALAEYTEVKTV 396
Cdd:cd07137 379 IVAETSSGGVTFNDTVVQYAidTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
114-402 |
2.54e-32 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 128.71 E-value: 2.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 114 LAAGFPPGVVNIVPGFGPTVGAaISSHPQINKIAFTGSTEVG-KLVKEAASRSnlKRVTLELGGKNPCIVCADADLDLAV 192
Cdd:PLN02419 300 MEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAGmHIYARAAAKG--KRIQSNMGAKNHGLVLPDANIDATL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 193 ECAHQGVFFNQGQCCTAASRV-FVEEQVYSEfvRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAK 271
Cdd:PLN02419 377 NALLAAGFGAAGQRCMALSTVvFVGDAKSWE--DKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAK 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 272 LECGGSAM----EDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKL 347
Cdd:PLN02419 455 LLLDGRDIvvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKF 534
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658310017 348 ASALESGTVWINcynaLYAQAPFGGFKMSGNGREL-------GEYALAEYTEVKTVTIKLGD 402
Cdd:PLN02419 535 QMDIEAGQIGIN----VPIPVPLPFFSFTGNKASFagdlnfyGKAGVDFFTQIKLVTQKQKD 592
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
112-397 |
1.37e-26 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 110.97 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 112 ATLAAGFP----PGVVNIVPGfGPTVGAAISSHPQiNKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIV-CADA 186
Cdd:PLN02203 152 AFLAANIPkyldSKAVKVIEG-GPAVGEQLLQHKW-DKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIVdSLSS 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 187 --DLDLAVE---------CAhqgvffnqGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTeQGPQIDQKQF 255
Cdd:PLN02203 229 srDTKVAVNrivggkwgsCA--------GQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHF 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 256 DKILELIESgKKEGAKLECGGSAMEDKgLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAA 335
Cdd:PLN02203 300 QRLSNLLKD-PRVAASIVHGGSIDEKK-LFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIY 377
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658310017 336 VFTKNLDKALKLASALESGTVWINCYNALYA--QAPFGGFKMSGNGRELGEYALAEYTEVKTVT 397
Cdd:PLN02203 378 AFTNNEKLKRRILSETSSGSVTFNDAIIQYAcdSLPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
111-379 |
7.11e-25 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 107.37 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 111 RATLAAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLV-KEAASR-SNLKRVT---LELGGKNPCIVCAD 185
Cdd:PRK11809 816 RILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLqRNLAGRlDPQGRPIpliAETGGQNAMIVDSS 895
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 186 ADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYS---EFVRRSV-EYAkkrpVGDPFDVKTEQGPQIDQKQFDKILEL 261
Cdd:PRK11809 896 ALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADrtlKMLRGAMaECR----MGNPDRLSTDIGPVIDAEAKANIERH 971
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 262 IESGKKEGAK---LECGGSAMEDKGLFIKPTVFsEVtDNMRIAKEEIFGPVQPILKFKS--IEEVIKRANSTDYGLTAAV 336
Cdd:PRK11809 972 IQAMRAKGRPvfqAARENSEDWQSGTFVPPTLI-EL-DSFDELKREVFGPVLHVVRYNRnqLDELIEQINASGYGLTLGV 1049
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 658310017 337 FTKNLDKALKLASALESGTVWI--NCYNALYAQAPFGGFKMSGNG 379
Cdd:PRK11809 1050 HTRIDETIAQVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
120-396 |
1.47e-20 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 93.19 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 120 PGVVNIVPGFGPTVGAAISShpQINKIAFTGSTEVGKLVKEAASRsNLKRVTLELGGKNPCIVCADADLDLAVECAHQGV 199
Cdd:PLN02174 168 SSAVRVVEGAVTETTALLEQ--KWDKIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGK 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 200 F-FNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKtEQGPQIDQKQFDKILELIESgKKEGAKLECGGSA 278
Cdd:PLN02174 245 WgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDRLSKLLDE-KEVSDKIVYGGEK 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 279 mEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWI 358
Cdd:PLN02174 323 -DRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVV 401
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 658310017 359 N---CYNALYAqAPFGGFKMSGNGRELGEYALAEYTEVKTV 396
Cdd:PLN02174 402 NdiaVHLALHT-LPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
119-359 |
5.47e-17 |
|
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: 82.29 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 119 PPGVVNIVPGFGPTvGAAISSHPQINKIAFTGSTEVGklvkeAASRSNLK--RVTLELGGKNPCIVCADADL--DLAVEC 194
Cdd:cd07084 157 PPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVA-----EKLALDAKqaRIYLELAGFNWKVLGPDAQAvdYVAWQC 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 195 AhQGVFFNQGQCCTAASRVFVEEQVYSE-FVRRSVEYAKKRPVGDpfdvkTEQGPQIdqkQFDKILELIESGKKEGAKLE 273
Cdd:cd07084 231 V-QDMTACSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLED-----LLLGPVQ---TFTTLAMIAHMENLLGSVLL 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 274 CGGSAM------EDKGLFIKPTVFSEVTDNMRIAK---EEIFGPVQPILKFKSIEE--VIKRANSTDYGLTAAVFTKNLD 342
Cdd:cd07084 302 FSGKELknhsipSIYGACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDPI 381
|
250
....*....|....*...
gi 658310017 343 KALKLASALES-GTVWIN 359
Cdd:cd07084 382 FLQELIGNLWVaGRTYAI 399
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
103-352 |
1.33e-15 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 78.21 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 103 LADLVErdratlAAGFPPGVVNIVPGfgptVGAAISSHPQ-INKIAFTGSTEVGKLVKE--AASRSNLkRVTLELGGKNP 179
Cdd:PRK11903 195 VKDVVA------AGILPAGALSVVCG----SSAGLLDHLQpFDVVSFTGSAETAAVLRShpAVVQRSV-RVNVEADSLNS 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 180 CIVCADAD-----LDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQ 254
Cdd:PRK11903 264 ALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 255 FDKILELIEsGKKEGAKLECGGSAME------DKGLFIKPTVF--SEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRAN 326
Cdd:PRK11903 344 LAAVRAGLA-ALRAQAEVLFDGGGFAlvdadpAVAACVGPTLLgaSDPDAATAVHDVEVFGPVATLLPYRDAAHALALAR 422
|
250 260
....*....|....*....|....*.
gi 658310017 327 STDYGLTAAVFTKnlDKALKLASALE 352
Cdd:PRK11903 423 RGQGSLVASVYSD--DAAFLAAAALE 446
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
103-352 |
1.10e-13 |
|
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: 72.19 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 103 LADLVER--DRATLAAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGK-LVKEAASRSNLKRVTLELGGKNP 179
Cdd:cd07129 149 TSELVARaiRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRaLFDAAAARPEPIPFYAELGSVNP 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 180 CIVCADADLDLAVECAhQG----VFFNQGQCCTAASRVFV-EEQVYSEFVRRSVEYAKKRPVGdpfdvkTEQGPQIdQKQ 254
Cdd:cd07129 229 VFILPGALAERGEAIA-QGfvgsLTLGAGQFCTNPGLVLVpAGPAGDAFIAALAEALAAAPAQ------TMLTPGI-AEA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 255 FDKILELIESGKkeGAKLECGGSAMEDKGLFiKPTVFSEVTDNMR---IAKEEIFGPVQPILKFKSIEEVIKRANSTDYG 331
Cdd:cd07129 301 YRQGVEALAAAP--GVRVLAGGAAAEGGNQA-APTLFKVDAAAFLadpALQEEVFGPASLVVRYDDAAELLAVAEALEGQ 377
|
250 260
....*....|....*....|...
gi 658310017 332 LTAAVF--TKNLDKALKLASALE 352
Cdd:cd07129 378 LTATIHgeEDDLALARELLPVLE 400
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
146-351 |
2.07e-13 |
|
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: 71.53 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 146 IAFTGSTEVG-KLVKEAASRSNLKRVTLELGGKNPCIVCADA-----DLDLAVECAHQGVFFNQGQCCTAASRVFVEEQV 219
Cdd:cd07128 225 VAFTGSAATAaKLRAHPNIVARSIRFNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEAR 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 220 YSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAME------DKGLFIKPTVF-S 292
Cdd:cd07128 305 VDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEvvgadaEKGAFFPPTLLlC 384
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 293 EVTDNMRIAKE-EIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASAL 351
Cdd:cd07128 385 DDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGA 444
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
131-352 |
6.64e-10 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 60.69 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 131 PTVGAA--ISSHPQINKIAFTGstevGKLVKEAASRSNlKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCT 208
Cdd:PRK15398 199 PTIETAqrLMKHPGIALLVVTG----GPAVVKAAMKSG-KKAIGAGAGNPPVVVDETADIEKAARDIVKGASFDNNLPCI 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 209 AASRVFVEEQVYSEFVRRsveyakkrpvgdpfdVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSA---MEDKGLF 285
Cdd:PRK15398 274 AEKEVIVVDSVADELMRL---------------MEKNGAVLLTAEQAEKLQKVVLKNGGTVNKKWVGKDAakiLEAAGIN 338
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658310017 286 IKPTV---FSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGL--TAAVFTKNLDKALKLASALE 352
Cdd:PRK15398 339 VPKDTrllIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHSRNVDNLNKMARAIQ 410
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
111-352 |
5.48e-09 |
|
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: 57.63 E-value: 5.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 111 RATLAAGFPPGVVNIVPGfgPTVGAA--ISSHPQINKIAFTGSTEVGKlvkeaASRSNLKRVTLELGGKNPCIVCADADL 188
Cdd:cd07121 149 KAIAEAGGPDNLVVTVEE--PTIETTneLMAHPDINLLVVTGGPAVVK-----AALSSGKKAIGAGAGNPPVVVDETADI 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 189 DLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRsveyakkrpvgdpfdVKTEQGPQIDQKQFDKILELIESGKKE 268
Cdd:cd07121 222 EKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAA---------------MQRNGAYVLNDEQAEQLLEVVLLTNKG 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 269 GA---KLEcGGSA---MEDKGLFIKPT---VFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGL--TAAVF 337
Cdd:cd07121 287 ATpnkKWV-GKDAskiLKAAGIEVPADirlIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIH 365
|
250
....*....|....*
gi 658310017 338 TKNLDKALKLASALE 352
Cdd:cd07121 366 SKNVENLTKMARAMQ 380
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
116-336 |
2.19e-07 |
|
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: 52.88 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 116 AGFPPGVVNIVPGFGPTVGAAIS-SHPQInkIAFTGSTEVGklvkEAASRSNLKRVTLELGGKNPCIVCAD-ADLDLAVE 193
Cdd:cd07126 195 CGMPATDVDLIHSDGPTMNKILLeANPRM--TLFTGSSKVA----ERLALELHGKVKLEDAGFDWKILGPDvSDVDYVAW 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 194 CAHQGVFFNQGQCCTAASRVFVEEQ-VYSEFVRRSVEYAKKRPVGDpfdvkTEQGP------QIDQKQFDKILELiesgk 266
Cdd:cd07126 269 QCDQDAYACSGQKCSAQSILFAHENwVQAGILDKLKALAEQRKLED-----LTIGPvltwttERILDHVDKLLAI----- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 267 kEGAKLECGGS------------AMEDKGLFIkPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEE--VIKRANSTDYGL 332
Cdd:cd07126 339 -PGAKVLFGGKpltnhsipsiygAYEPTAVFV-PLEEIAIEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHL 416
|
....
gi 658310017 333 TAAV 336
Cdd:cd07126 417 TAAV 420
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
112-372 |
2.18e-05 |
|
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: 46.45 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 112 ATLAAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVgklVKEAASRSNLKRVTLELGGKNPCIVCADADLDLA 191
Cdd:cd07077 151 AADAAHGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDA---VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 192 VECAHQGVFFNQGQCctaasrvFVEEQVYSefvrrsveyakkrpVGDPFDVKTEQgpqidqkqfdkileLIESGKKEGAK 271
Cdd:cd07077 228 SGSVHDSKFFDQNAC-------ASEQNLYV--------------VDDVLDPLYEE--------------FKLKLVVEGLK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 272 LECGgsamedkglfIKPtVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRA----NSTDYGLTAAVFTKNLDKALKL 347
Cdd:cd07077 273 VPQE----------TKP-LSKETTPSFDDEALESMTPLECQFRVLDVISAVENAwmiiESGGGPHTRCVYTHKINKVDDF 341
|
250 260
....*....|....*....|....*
gi 658310017 348 ASALESGTVWINCYNALYAQAPFGG 372
Cdd:cd07077 342 VQYIDTASFYPNESSKKGRGAFAGK 366
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
103-215 |
1.14e-04 |
|
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: 44.39 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658310017 103 LADLVERDRATLA-AGFPPGVVNIV---PGFGptVGAAISSHPQINKIAFTGSTEVGKLVKEAASRsnlKRVTLELGGKN 178
Cdd:cd07127 236 LAITVQVAREVLAeAGFDPNLVTLAadtPEEP--IAQTLATRPEVRIIDFTGSNAFGDWLEANARQ---AQVYTEKAGVN 310
|
90 100 110
....*....|....*....|....*....|....*....
gi 658310017 179 PCIVcaDADLDLAVECAHQGVFFN--QGQCCTAASRVFV 215
Cdd:cd07127 311 TVVV--DSTDDLKAMLRNLAFSLSlySGQMCTTPQNIYV 347
|
|
| |
