|
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 ... |
42-276 |
5.28e-168 |
|
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: 474.14 E-value: 5.28e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 42 KKAKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGSPWRRLDALSRGQLLHQLADLVER 121
Cdd:cd07141 5 KYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLADLIER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 122 DRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAW 201
Cdd:cd07141 85 DRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAW 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148675271 202 KLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVSPL 276
Cdd:cd07141 165 KLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKL 239
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
45-273 |
1.97e-145 |
|
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: 416.61 E-value: 1.97e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 45 KIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGSpWRRLDALSRGQLLHQLADLVERDRA 124
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIERDRD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 125 ILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLA 204
Cdd:cd07091 84 ELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148675271 205 PALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07091 164 PALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAV 232
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
45-273 |
2.60e-118 |
|
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: 348.24 E-value: 2.60e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 45 KIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgSPWRRLDALSRGQLLHQLADLVERDRA 124
Cdd:cd07144 9 GLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEKNRD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 125 ILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLA 204
Cdd:cd07144 87 LLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148675271 205 PALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07144 167 PALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTAT 235
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
42-273 |
6.54e-109 |
|
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: 323.68 E-value: 6.54e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 42 KKAKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLVER 121
Cdd:cd07142 2 KHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 122 DRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAW 201
Cdd:cd07142 81 HADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAW 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148675271 202 KLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07142 161 KVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEV 232
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
40-273 |
8.10e-109 |
|
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: 323.62 E-value: 8.10e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 40 TMKKAKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLV 119
Cdd:COG1012 2 TTPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 120 ERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLM 198
Cdd:COG1012 79 EERREELAALLTLETGKPLAEARG-EVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148675271 199 LAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:COG1012 158 AAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAV 232
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
46-273 |
1.04e-108 |
|
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: 323.33 E-value: 1.04e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 46 IFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgSPWRR-LDALSRGQLLHQLADLVERDRA 124
Cdd:cd07143 9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWGLkVSGSKRGRCLSKLADLMERNLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 125 ILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLA 204
Cdd:cd07143 87 YLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148675271 205 PALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07143 167 PALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLV 235
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
52-273 |
1.32e-105 |
|
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: 314.85 E-value: 1.32e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 52 WHESkSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLET 131
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 132 MDTGKPFLHAFFvDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGN 211
Cdd:pfam00171 77 LENGKPLAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148675271 212 TVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAV 217
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
33-281 |
2.15e-99 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 301.34 E-value: 2.15e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 33 PLQRPLRtMKKAKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLL 112
Cdd:PLN02466 48 PITPPVQ-VSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEG-PWPKMTAYERSRIL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 113 HQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPW 192
Cdd:PLN02466 126 LRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPW 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 193 NFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTE 272
Cdd:PLN02466 206 NFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTD 285
|
....*....
gi 148675271 273 VSPLCELLA 281
Cdd:PLN02466 286 TGKIVLELA 294
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
47-273 |
8.27e-99 |
|
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: 298.07 E-value: 8.27e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 47 FINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLVERDRAIL 126
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSG-EWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 127 ATLETMDTGKPFLHAFFvDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPA 206
Cdd:cd07119 80 ARLETLNTGKTLRESEI-DIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148675271 207 LCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTAT 225
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
63-273 |
6.43e-98 |
|
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: 295.23 E-value: 6.43e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 63 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFqRGSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAF 142
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAF-EGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKL-IRET 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 143 FVDLEGCIKTFRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQT 221
Cdd:cd07114 79 RAQVRYLAEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 148675271 222 PLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07114 159 PASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTET 210
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
58-273 |
4.76e-95 |
|
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: 287.96 E-value: 4.76e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 58 GRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGSpWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKP 137
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 138 FLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKP 217
Cdd:cd07112 80 ISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 148675271 218 AEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEV 215
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
45-273 |
7.28e-94 |
|
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: 285.54 E-value: 7.28e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 45 KIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLVERDRA 124
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENG-EWGKMNARDRGRLMYRLADLMEEHQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 125 ILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTD----DNVVCFTRHEPIGVCGAITPWNFPLLMLA 200
Cdd:cd07140 86 ELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNYPLMMLA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148675271 201 WKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07140 166 WKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPI 238
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
63-273 |
1.95e-91 |
|
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: 278.55 E-value: 1.95e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 63 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF 142
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 143 FVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTP 222
Cdd:cd07115 78 RLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148675271 223 LTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAV 208
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
40-273 |
6.85e-89 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 273.24 E-value: 6.85e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 40 TMKKAKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLV 119
Cdd:PLN02766 17 EIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 120 ERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLML 199
Cdd:PLN02766 96 EEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMF 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148675271 200 AWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:PLN02766 176 FMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEV 249
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
84-273 |
2.58e-87 |
|
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: 267.15 E-value: 2.58e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 84 DKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAFFVDLEGCIKTFRYFAGWADKI 163
Cdd:cd07078 1 DAAVAAARAAFKA---WAALPPAERAAILRKLADLLEERREELAALETLETGKP-IEEALGEVARAADTFRYYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 164 QGRTIPTDD-NVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVV 242
Cdd:cd07078 77 HGEVIPSPDpGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190
....*....|....*....|....*....|.
gi 148675271 243 NIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAV 187
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
45-273 |
1.23e-86 |
|
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: 266.90 E-value: 1.23e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 45 KIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRA 124
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT---WGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 125 ILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLA 204
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148675271 205 PALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTV 226
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
63-272 |
1.81e-86 |
|
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: 265.58 E-value: 1.81e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 63 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF 142
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG---WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 143 FVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTP 222
Cdd:cd07093 78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 148675271 223 LTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTE 272
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETA 207
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
64-273 |
3.93e-83 |
|
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: 257.16 E-value: 3.93e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 64 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFf 143
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESG--WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 144 VDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPL 223
Cdd:cd07109 79 ADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 148675271 224 TALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVET 208
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
88-273 |
5.99e-81 |
|
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: 248.68 E-value: 5.99e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 88 EAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAFFVDLEGCIKTFRYFAGWADKIQGRT 167
Cdd:cd06534 1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKP-IEEALGEVARAIDTFRYAAGLADKLGGPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 168 IP-TDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVP 246
Cdd:cd06534 77 LPsPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
|
170 180
....*....|....*....|....*..
gi 148675271 247 GFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAV 183
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
45-273 |
9.20e-79 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 246.36 E-value: 9.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 45 KIFINNDWhESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRA 124
Cdd:PRK13473 4 KLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE---WSQTTPKERAEALLKLADAIEENAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 125 ILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTipTDDNVVCFT---RHEPIGVCGAITPWNFPLLMLAW 201
Cdd:PRK13473 80 EFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKA--AGEYLEGHTsmiRRDPVGVVASIAPWNYPLMMAAW 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148675271 202 KLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:PRK13473 158 KLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIAT 228
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
64-273 |
1.33e-77 |
|
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: 242.72 E-value: 1.33e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 64 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFf 143
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 144 VDLEGCIKTFRYFAGWADKIQGRTIPTDD-NVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTP 222
Cdd:cd07103 78 GEVDYAASFLEWFAEEARRIYGRTIPSPApGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148675271 223 LTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAV 208
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
36-273 |
2.81e-77 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 243.26 E-value: 2.81e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 36 RPLRTMKKAKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGSpWRRLDALSRGQLLHQL 115
Cdd:PRK09847 12 KALSLAIENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 116 ADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFP 195
Cdd:PRK09847 91 ADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148675271 196 LLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:PRK09847 171 LLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRT 248
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
45-273 |
2.97e-76 |
|
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: 240.05 E-value: 2.97e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 45 KIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRA 124
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT---WRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 125 ILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLA 204
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148675271 205 PALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEV 226
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
47-272 |
1.25e-75 |
|
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: 238.32 E-value: 1.25e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 47 FINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQLADLVERDRAIL 126
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAA-QKA--WERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 127 ATLETMDTGKPFLHAFfVDLEGCIKTFRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAP 205
Cdd:cd07088 78 AKLIVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDrPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148675271 206 ALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTE 272
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTE 223
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
47-273 |
3.35e-75 |
|
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: 237.29 E-value: 3.35e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 47 FINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAIL 126
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES---WSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 127 ATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQgrtipTDdnvvcFTRHEPIGVCGAITPWNFPLLMLAWKLAPA 206
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLD-----TE-----LAGWKPVGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148675271 207 LCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTG-NGSFGSALANHPGVDKVAFTGSTEV 237
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
47-283 |
1.28e-74 |
|
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: 235.70 E-value: 1.28e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 47 FINNDWHESKSGRKFATYNPSTLEKIC-EVEEGDKPDVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAI 125
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVVgTFPLSTASDVDAAVEAAREAF---PEWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 126 LATLETMDTGKPFLHAFfVDLEGCIKTFRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLA 204
Cdd:cd07131 79 LARLVTREMGKPLAEGR-GDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148675271 205 PALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVSplcELLAET 283
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVG---ERIGET 233
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
64-273 |
1.45e-74 |
|
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: 234.91 E-value: 1.45e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 64 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFF 143
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPS---WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 144 VDLEGCIKTFRYFAGWADKIQGRT----IPtddNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAE 219
Cdd:cd07092 79 DELPGAVDNFRFFAGAARTLEGPAageyLP---GHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 148675271 220 QTPLTALYLASLIKEVgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07092 156 TTPLTTLLLAELAAEV-LPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRT 208
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
63-273 |
4.34e-74 |
|
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: 233.78 E-value: 4.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 63 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAF 142
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR---WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKP-LDEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 143 FVDLEGCIKTFRYFAGWADKI---QGRTIPTDDN-VVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPA 218
Cdd:cd07110 77 AWDVDDVAGCFEYYADLAEQLdakAERAVPLPSEdFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 148675271 219 EQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTAT 211
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
38-272 |
4.30e-72 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 229.38 E-value: 4.30e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 38 LRTMKKAKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLAD 117
Cdd:PRK13252 1 MSRQPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 118 LV-ERDRAiLATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPL 196
Cdd:PRK13252 78 ILrERNDE-LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148675271 197 LMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGpTVGAAISSHPQINKIAFTGSTE 272
Cdd:PRK13252 157 QIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVP 231
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
47-272 |
4.31e-72 |
|
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: 228.93 E-value: 4.31e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 47 FINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAIL 126
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGE---WAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 127 ATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPA 206
Cdd:TIGR01804 78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148675271 207 LCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTE 272
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVP 223
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
64-273 |
5.25e-72 |
|
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: 228.18 E-value: 5.25e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 64 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFF 143
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG---WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 144 vDLEGCIKTFRYFAGWAdkIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPL 223
Cdd:cd07106 79 -EVGGAVAWLRYTASLD--LPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 148675271 224 TALYLASLIKEVgFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTAT 203
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
47-273 |
9.45e-72 |
|
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: 228.29 E-value: 9.45e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 47 FINNDWHESKSGRkfATYNPSTL-EKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAI 125
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSDTsDVVGKYARASAEDADAAIAAAAAAFPA---WRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 126 LATLETMDTGKPFLHAFFvDLEGCIKTFRYFAGWADKIQGRTIP-TDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLA 204
Cdd:cd07097 79 LARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148675271 205 PALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAV 226
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
65-273 |
4.64e-71 |
|
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: 226.09 E-value: 4.64e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 65 NPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFV 144
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 145 DLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLT 224
Cdd:cd07108 80 EAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 148675271 225 ALYLASLIKEVgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEV 207
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
47-276 |
8.82e-71 |
|
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: 225.79 E-value: 8.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 47 FINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAIL 126
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA---WGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 127 ATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPA 206
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 207 LCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVSPL 276
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRL 229
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
46-273 |
2.57e-70 |
|
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: 224.30 E-value: 2.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 46 IFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAF---QRGSPWRRLDALSRgqllhqLADLVERD 122
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFpawSATSVEERAALLER------IAEAYEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 123 RAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVcftrHEPIGVCGAITPWNFPLLMLAWK 202
Cdd:cd07138 75 ADELAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEFEERRGNSLVV----REPIGVCGLITPWNWPLNQIVLK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148675271 203 LAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07138 151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRA 221
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
44-272 |
1.19e-69 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 223.84 E-value: 1.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 44 AKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQR--GSPWRRLDALSRGQLLHQLADLVER 121
Cdd:PLN02467 8 RQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkGKDWARTTGAVRAKYLRAIAAKITE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 122 DRAILATLETMDTGKPFLHAFF--VDLEGCiktFRYFAGWADKIQGR-----TIPtDDNVVCFTRHEPIGVCGAITPWNF 194
Cdd:PLN02467 88 RKSELAKLETLDCGKPLDEAAWdmDDVAGC---FEYYADLAEALDAKqkapvSLP-METFKGYVLKEPLGVVGLITPWNY 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148675271 195 PLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTE 272
Cdd:PLN02467 164 PLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTA 241
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
63-273 |
2.57e-69 |
|
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: 221.41 E-value: 2.57e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 63 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF 142
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 143 fVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTP 222
Cdd:cd07090 78 -VDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148675271 223 LTALYLASLIKEVGFPPGVVNIVPGFGPTvGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPT 206
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
46-273 |
2.86e-67 |
|
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: 216.67 E-value: 2.86e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 46 IFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLVERDRAI 125
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 126 LATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADK---IQGRTIPTDDNVVcfTRHEPIGVCGAITPWNFPLLMLAWK 202
Cdd:cd07139 80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDfpfEERRPGSGGGHVL--VRREPVGVVAAIVPWNAPLFLAALK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148675271 203 LAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07139 158 IAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAA 227
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
47-271 |
7.74e-66 |
|
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: 213.07 E-value: 7.74e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 47 FINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgSPWRRLDALSRGQLLHQLADLVERDRAIL 126
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 127 ATLETMDTGKPFLHAFFVDLEGCIKTFRYFAGWADKIQGRTI------PTDDNVVCFTRHEPIGVCGAITPWNFPLLMLA 200
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLapsipsMQGERYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148675271 201 WKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGpTVGAAISSHPQINKIAFTGST 271
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSV 230
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
64-273 |
1.47e-65 |
|
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: 211.72 E-value: 1.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 64 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGsPWRRlDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFF 143
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTG-DWST-DAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 144 VDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVC-----FTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPA 218
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFPWEFDLPVPALRGgpgrrVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 148675271 219 EQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAV 214
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
43-273 |
1.64e-64 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 210.32 E-value: 1.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 43 KAKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERD 122
Cdd:PLN02278 24 RTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLTASERSKILRRWYDLIIAN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 123 RAILATLETMDTGKPFLHAF--------FVDlegciktfrYFAGWADKIQGRTIPTDD-NVVCFTRHEPIGVCGAITPWN 193
Cdd:PLN02278 101 KEDLAQLMTLEQGKPLKEAIgevaygasFLE---------YFAEEAKRVYGDIIPSPFpDRRLLVLKQPVGVVGAITPWN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 194 FPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:PLN02278 172 FPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAV 251
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
61-273 |
1.67e-64 |
|
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: 209.13 E-value: 1.67e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 61 FATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLH 140
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV---MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 141 AFfVDLEGCIKTFRYFAGWADKIQGRTIPTDD-----NVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVL 215
Cdd:cd07145 78 SR-VEVERTIRLFKLAAEEAKVLRGETIPVDAyeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 148675271 216 KPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAV 214
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
63-271 |
7.53e-64 |
|
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: 207.23 E-value: 7.53e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 63 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAF 142
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE---WRATTPLERARMLRELATRLREHAEELALIDALDCGNP-VSAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 143 FVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTP 222
Cdd:cd07107 77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 148675271 223 LTALYLASLIKEVgFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGST 271
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSV 204
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
47-273 |
1.07e-61 |
|
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: 202.41 E-value: 1.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 47 FINNDWHESKSGRkFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAIL 126
Cdd:cd07086 2 VIGGEWVGSGGET-FTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE---WRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 127 ATLETMDTGKPFLHAF-----FVDLegCIktfrYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLA 200
Cdd:cd07086 78 GRLVSLEMGKILPEGLgevqeMIDI--CD----YAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148675271 201 WKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV----GFPPGVVNIVPGFGPtVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07086 152 WNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEV 227
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
77-273 |
2.77e-61 |
|
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: 200.64 E-value: 2.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 77 EGDKPDVDKAVEAAQAAFQRGsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYF 156
Cdd:cd07118 15 EGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQAR-GEIEGAADLWRYA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 157 AGWADKIQGRTIPT-DDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV 235
Cdd:cd07118 93 ASLARTLHGDSYNNlGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEA 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 148675271 236 GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07118 173 GLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRV 210
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
47-271 |
1.23e-60 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 199.56 E-value: 1.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 47 FINNDWHESksGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGsPWRRLDALSRGQLLHQLADLVERDRAIL 126
Cdd:TIGR03216 4 FINGAFVES--GKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAA-LKG-PWGKMTVAERADLLYAVADEIERRFDDF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 127 ATLETMDTGKPFLHAFFVDLEGCIKTFRYFAgwaDKIqgRTIPTD---------DNVVCFTRHEPIGVCGAITPWNFPLL 197
Cdd:TIGR03216 80 LAAEVADTGKPRSLASHLDIPRGAANFRVFA---DVV--KNAPTEcfematpdgKGALNYAVRKPLGVVGVISPWNLPLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148675271 198 MLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGP-TVGAAISSHPQINKIAFTGST 271
Cdd:TIGR03216 155 LMTWKVGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPdSAGEFLTRHPGVDAITFTGET 229
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
64-273 |
5.18e-60 |
|
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: 197.43 E-value: 5.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 64 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGspwRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAFF 143
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKP-IKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 144 VDLEGCIKTFRYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPA 218
Cdd:cd07149 80 KEVDRAIETLRLSAEEAKRLAGETIPFDaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 148675271 219 EQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAV 214
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
45-273 |
1.29e-59 |
|
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: 196.97 E-value: 1.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 45 KIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRA 124
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA---WSATPVLKRQQVMFKFRQLLEENLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 125 ILATLETMDTGKPFLHAFfVDLEGCIKTFRYFAGWADKIQGRTIP-TDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKL 203
Cdd:cd07085 79 ELARLITLEHGKTLADAR-GDVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 204 APALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGaAISSHPQINKIAFTGSTEV 273
Cdd:cd07085 158 PMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVN-ALLDHPDIKAVSFVGSTPV 226
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
46-273 |
1.87e-56 |
|
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: 189.36 E-value: 1.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 46 IFINNDwhESKSGRKFATYNPS-TLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRA 124
Cdd:cd07124 35 LVIGGK--EVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPT---WRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 125 ILATLETMDTGKPFLHAFfVDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLA 204
Cdd:cd07124 110 ELAAWMVLEVGKNWAEAD-ADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148675271 205 PALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREV 257
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
61-273 |
1.91e-53 |
|
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: 180.22 E-value: 1.91e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 61 FATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLH 140
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 141 AFFvDLEGCIKTFRYFAGWADKIQGRTIPTDDN-VVCFTRHEPIGVCGAITPWNFPLLmLAWK-LAPALCCGNTVVLKPA 218
Cdd:cd07150 78 AWF-ETTFTPELLRAAAGECRRVRGETLPSDSPgTVSMSVRRPLGVVAGITPFNYPLI-LATKkVAFALAAGNTVVLKPS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 148675271 219 EQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07150 156 EETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAV 210
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
64-273 |
2.07e-53 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 179.93 E-value: 2.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 64 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAff 143
Cdd:TIGR01780 2 YNPATGEIIGSVPDQGVDETEAAIRAAYEAFKT---WRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 144 vdlEGCIKT----FRYFAGWADKIQGRTIPT--DDNVVCFTRhEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKP 217
Cdd:TIGR01780 77 ---KGEILYaasfLEWFAEEAKRVYGDTIPSpqSDKRLIVIK-QPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148675271 218 AEQTPLTALYLASLIKEVGFPPGVVNIVPG-FGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:TIGR01780 153 AEQTPLSALALARLAEQAGIPKGVLNVITGsRAKEVGNVLTTSPLVRKISFTGSTNV 209
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
63-273 |
2.95e-53 |
|
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: 179.85 E-value: 2.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 63 TYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFqRGSPWRRlDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF 142
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAF-DETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 143 FvDLEGCIKTFRYFAGWADKIQGRTI-PTDDNVVCFTRhEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQT 221
Cdd:cd07120 79 F-EISGAISELRYYAGLARTEAGRMIePEPGSFSLVLR-EPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 148675271 222 PLTALYLASLIKEV-GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07120 157 AQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTAT 209
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
65-273 |
1.71e-52 |
|
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: 177.63 E-value: 1.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 65 NPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfV 144
Cdd:cd07094 5 NPYDGEVIGKVPADDRADAEEALATARAGAEN---RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR-V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 145 DLEGCIKTFRYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAE 219
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 148675271 220 QTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAV 214
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
82-273 |
9.71e-51 |
|
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: 172.33 E-value: 9.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 82 DVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYFAGWAD 161
Cdd:cd07104 1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAF-EVGAAIAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 162 KIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLmLAWK-LAPALCCGNTVVLKPAEQTPLT-ALYLASLIKEVGFP 238
Cdd:cd07104 77 RPEGEILPSDvPGKESMVRRVPLGVVGVISPFNFPLI-LAMRsVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLP 155
|
170 180 190
....*....|....*....|....*....|....*
gi 148675271 239 PGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07104 156 KGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAV 190
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
45-273 |
5.20e-48 |
|
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: 166.21 E-value: 5.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 45 KIFINNDWHESkSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGSpWRRLDALSRGQLLHQLADLVERDRA 124
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDA-GRGW-WPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 125 ILATLETMDTGKPflhaffvdLEGCIKTF-------RYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPW 192
Cdd:cd07082 80 EVANLLMWEIGKT--------LKDALKEVdrtidyiRDTIEELKRLDGDSLPGDwfpgtKGKIAQVRREPLGVVLAIGPF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 193 NFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTE 272
Cdd:cd07082 152 NYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTE 231
|
.
gi 148675271 273 V 273
Cdd:cd07082 232 V 232
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
40-273 |
1.22e-46 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 162.77 E-value: 1.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 40 TMKKAKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLV 119
Cdd:PRK11241 7 TLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRAL---PAWRALTAKERANILRRWFNLM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 120 ERDRAILATLETMDTGKPFLHAffvdlEGCIKTFRYFAGW----ADKIQGRTIP---TDDNVVCFTrhEPIGVCGAITPW 192
Cdd:PRK11241 84 MEHQDDLARLMTLEQGKPLAEA-----KGEISYAASFIEWfaeeGKRIYGDTIPghqADKRLIVIK--QPIGVTAAITPW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 193 NFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTE 272
Cdd:PRK11241 157 NFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTE 236
|
.
gi 148675271 273 V 273
Cdd:PRK11241 237 I 237
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
54-283 |
1.27e-44 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 161.64 E-value: 1.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 54 ESKSGRKFATYNPSTLEKIC-EVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETM 132
Cdd:COG4230 565 EAASGEARPVRNPADHSDVVgTVVEATAADVEAALAAAQAAFPA---WSATPVEERAAILERAADLLEAHRAELMALLVR 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 133 DTGKPFLHAF-----FVDLegCiktfRYFAGwadkiQGRTIPTDDnvvcfTRHEPIGVCGAITPWNFPLLMLAWKLAPAL 207
Cdd:COG4230 642 EAGKTLPDAIaevreAVDF--C----RYYAA-----QARRLFAAP-----TVLRGRGVFVCISPWNFPLAIFTGQVAAAL 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 208 CCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV------------SP 275
Cdd:COG4230 706 AAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETarlinrtlaardGP 785
|
....*...
gi 148675271 276 LCELLAET 283
Cdd:COG4230 786 IVPLIAET 793
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
60-273 |
1.56e-44 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 157.79 E-value: 1.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 60 KFATYNPS-TLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPF 138
Cdd:PRK03137 51 KIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFET---WKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPW 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 139 LHAFfVDLEGCIKTFRYFA----GWADKIQGRTIPTDDNvvcFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVV 214
Cdd:PRK03137 128 AEAD-ADTAEAIDFLEYYArqmlKLADGKPVESRPGEHN---RYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 148675271 215 LKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:PRK03137 204 LKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREV 262
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
64-273 |
1.70e-44 |
|
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: 156.64 E-value: 1.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 64 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFF 143
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 144 vDLEGCIKTFRYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPA 218
Cdd:cd07147 81 -EVARAIDTFRIAAEEATRIYGEVLPLDisargEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 148675271 219 EQTPLTALYLASLIKEVGFPPGVVNIVPgfGPTVGAAI-SSHPQINKIAFTGSTEV 273
Cdd:cd07147 160 SRTPLSALILGEVLAETGLPKGAFSVLP--CSRDDADLlVTDERIKLLSFTGSPAV 213
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
82-273 |
1.47e-43 |
|
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: 153.50 E-value: 1.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 82 DVDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYFAGWAD 161
Cdd:cd07105 1 DADQAVEAAAAAFP---AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGF-NVDLAAGMLREAASLIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 162 KIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPG 240
Cdd:cd07105 77 QIIGGSIPSDkPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKG 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 148675271 241 VVNIV---PGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07105 157 VLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRV 192
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
64-271 |
2.70e-43 |
|
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: 153.15 E-value: 2.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 64 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAFF 143
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAA-QRA--WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 144 VDLEGCIKTFRYFAGWADKI-QGRTIPTDD---NVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAE 219
Cdd:cd07099 77 LEVLLALEAIDWAARNAPRVlAPRKVPTGLlmpNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 148675271 220 QTPLTALYLASLIKEVGFPPGVVNIVPGFGPTvGAAISSHPqINKIAFTGST 271
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSV 206
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
64-283 |
4.05e-43 |
|
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: 153.89 E-value: 4.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 64 YNPSTLEK-ICEVEEGDKPDVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF 142
Cdd:cd07125 51 IDPADHERtIGEVSLADAEDVDAALAIAAAAF---AGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADAD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 143 -----FVDLegCiktfRYFAGWADKIQGRTI---PTD--DNVVCftrhEPIGVCGAITPWNFPLLMLAWKLAPALCCGNT 212
Cdd:cd07125 128 aevreAIDF--C----RYYAAQARELFSDPElpgPTGelNGLEL----HGRGVFVCISPWNFPLAIFTGQIAAALAAGNT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 213 VVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV------------SPLCELL 280
Cdd:cd07125 198 VIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETaklinralaerdGPILPLI 277
|
...
gi 148675271 281 AET 283
Cdd:cd07125 278 AET 280
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
54-272 |
5.02e-43 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 153.88 E-value: 5.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 54 ESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQLADLVERDRAILATLETMD 133
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA-QRA--WAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 134 TGKPFLHAF--FVDLEGCIktfRYFAGWADKI------QGrTIPTDDNVVcfTRHEPIGVCGAITPWNFPLLMLAWKLAP 205
Cdd:PRK09407 104 TGKARRHAFeeVLDVALTA---RYYARRAPKLlaprrrAG-ALPVLTKTT--ELRQPKGVVGVISPWNYPLTLAVSDAIP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148675271 206 ALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHpqINKIAFTGSTE 272
Cdd:PRK09407 178 ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTA 242
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
50-273 |
6.02e-43 |
|
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: 152.84 E-value: 6.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 50 NDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRgsPWRRLDALSRGQLLHQLADLVERDRAILATL 129
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA-QK--EWAATLPQERAEILEKAAQILEERRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 130 ETMDTGKPFLHAFFvDLEGCIKTFRYFAGWADKIQGRTIPTD----DNVVcftRHEPIGVCGAITPWNFPLLMLAWKLAP 205
Cdd:cd07151 78 LIRESGSTRIKANI-EWGAAMAITREAATFPLRMEGRILPSDvpgkENRV---YREPLGVVGVISPWNFPLHLSMRSVAP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148675271 206 ALCCGNTVVLKPAEQTPLTA-LYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07151 154 ALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPV 222
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
65-273 |
2.76e-42 |
|
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: 150.59 E-value: 2.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 65 NPSTLEKICEVEEGDKPDVDKAVEAAqaafqrGSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfV 144
Cdd:cd07146 5 NPYTGEVVGTVPAGTEEALREALALA------ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR-Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 145 DLEGCIKTFRYFAGWADKIQGRTIPTDDNV-----VCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAE 219
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGESFSCDLTAngkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 148675271 220 QTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAV 211
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
43-283 |
5.60e-42 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 153.82 E-value: 5.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 43 KAKIFINNDwhesksGRKFATYNPSTLEK-ICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVER 121
Cdd:PRK11904 552 QAGPIINGE------GEARPVVSPADRRRvVGEVAFADAEQVEQALAAARAAFPA---WSRTPVEERAAILERAADLLEA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 122 DRAILATLETMDTGKPfLH--------AffVDLegCiktfRYFAGWADKIQGRTI----PT-DDNVVcftRHEPIGVCGA 188
Cdd:PRK11904 623 NRAELIALCVREAGKT-LQdaiaevreA--VDF--C----RYYAAQARRLFGAPEklpgPTgESNEL---RLHGRGVFVC 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 189 ITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFT 268
Cdd:PRK11904 691 ISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFT 770
|
250 260
....*....|....*....|....*..
gi 148675271 269 GSTEV------------SPLCELLAET 283
Cdd:PRK11904 771 GSTETariinrtlaardGPIVPLIAET 797
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
57-271 |
7.47e-42 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 149.92 E-value: 7.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 57 SGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgSPWRRLDALsRGQLLHQLADLVERDRAILATLETMDTGK 136
Cdd:TIGR04284 13 SAGTFPTVNPATEEVLGVAADATAADMDAAIAAARRAFDE-TDWSRDTAL-RVRCLRQLRDALRAHVEELRELTIAEVGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 137 PFLHAFFVDLEGCIKTFRYFAGWADKIQGRT---------IPTDDNVvcftRHEPIGVCGAITPWNFPLLMLAWKLAPAL 207
Cdd:TIGR04284 91 PRMLTAGAQLEGPVDDLGFAADLAESYAWTTdlgvaspmgIPTRRTL----RREAVGVVGAITPWNFPHQINLAKLGPAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148675271 208 CCGNTVVLKPAEQTPLTALYLASLIKE-VGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGST 271
Cdd:TIGR04284 167 AAGNTVVLKPAPDTPWCAAVLGELIAEhTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGST 231
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
38-273 |
3.68e-41 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 151.56 E-value: 3.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 38 LRTMKKA-KIFINNDWH-------ESKSGRKFATYNPS-TLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSR 108
Cdd:PRK11905 538 LAALDEAlNAFAAKTWHaapllagGDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPE---WSATPAAER 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 109 GQLLHQLADLVERDRAILATLETMDTGKPFLHAF-----FVDlegciktF-RYFAGwadkiQGRTIPTDDnvvcftRHEP 182
Cdd:PRK11905 615 AAILERAADLMEAHMPELFALAVREAGKTLANAIaevreAVD-------FlRYYAA-----QARRLLNGP------GHKP 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 183 IGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQI 262
Cdd:PRK11905 677 LGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRI 756
|
250
....*....|.
gi 148675271 263 NKIAFTGSTEV 273
Cdd:PRK11905 757 AGVMFTGSTEV 767
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
72-276 |
6.06e-41 |
|
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: 148.13 E-value: 6.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 72 ICEVEEGDKPDVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFlHAFFVDLEGCIK 151
Cdd:TIGR01238 65 VGQVFHANLAHVQAAIDSAQQAF---PTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTI-HNAIAEVREAVD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 152 TFRYFAGWADKiqgrTIPTDDnvvcftrHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASL 231
Cdd:TIGR01238 141 FCRYYAKQVRD----VLGEFS-------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVEL 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 148675271 232 IKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVSPL 276
Cdd:TIGR01238 210 MQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQL 254
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
70-273 |
7.25e-41 |
|
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: 146.67 E-value: 7.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 70 EKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFFvDLEGC 149
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAA-QRA--WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGF-EVGAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 150 IKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTA-LYL 228
Cdd:cd07152 78 IGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 148675271 229 ASLIKEVGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAV 201
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
33-273 |
1.86e-39 |
|
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: 143.87 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 33 PLQRPLRTMKKAK-----IFINNDWHESKSgRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALS 107
Cdd:cd07083 3 AMREALRRVKEEFgraypLVIGGEWVDTKE-RMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKT---WKDWPQED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 108 RGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYFAGWADKIQGR-----TIPTDDNVvcfTRHEP 182
Cdd:cd07083 79 RARLLLKAADLLRRRRRELIATLTYEVGKNWVEAI-DDVAEAIDFIRYYARAALRLRYPavevvPYPGEDNE---SFYVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 183 IGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQI 262
Cdd:cd07083 155 LGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERI 234
|
250
....*....|.
gi 148675271 263 NKIAFTGSTEV 273
Cdd:cd07083 235 RGINFTGSLET 245
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
49-273 |
3.16e-39 |
|
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: 142.73 E-value: 3.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 49 NNDWheSKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILAT 128
Cdd:cd07130 4 DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE---WRDVPAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 129 LETMDTGKPFLHAF-----FVDLegCiktfRYFAGWADKIQGRTIPTD--DNVVCFTRHePIGVCGAITPWNFPLLMLAW 201
Cdd:cd07130 79 LVSLEMGKILPEGLgevqeMIDI--C----DFAVGLSRQLYGLTIPSErpGHRMMEQWN-PLGVVGVITAFNFPVAVWGW 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148675271 202 KLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV----GFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07130 152 NAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAV 226
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
112-272 |
4.88e-38 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 138.33 E-value: 4.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 112 LHQLADLVERDRAILATLETMDTGKPFLHAFfVDLEGCIKTFRYFAGWADKIQGRTIPTD---DNVVCFTRhePIGVCGA 188
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAE-VEVAFTADYIDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 189 ITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFT 268
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
....
gi 148675271 269 GSTE 272
Cdd:PRK10090 158 GSVS 161
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
66-271 |
7.26e-38 |
|
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: 138.98 E-value: 7.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 66 PSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF--F 143
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA-QRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFeeV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 144 VDlegCIKTFRYFAGWADKI-----QGRTIPT-DDNVVCftrHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKP 217
Cdd:cd07101 80 LD---VAIVARYYARRAERLlkprrRRGAIPVlTRTTVN---RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 148675271 218 AEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHpqINKIAFTGST 271
Cdd:cd07101 154 DSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGST 205
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
83-271 |
1.04e-37 |
|
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: 137.98 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 83 VDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFF-VDLegCIKTFRYFAGWAD 161
Cdd:cd07100 1 IEAALDRAHAAFLA---WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAeVEK--CAWICRYYAENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 162 K-IQGRTIPTDDNVvCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPG 240
Cdd:cd07100 76 AfLADEPIETDAGK-AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEG 154
|
170 180 190
....*....|....*....|....*....|.
gi 148675271 241 VVNIVPGFGPTVGAAIsSHPQINKIAFTGST 271
Cdd:cd07100 155 VFQNLLIDSDQVEAII-ADPRVRGVTLTGSE 184
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
46-273 |
2.51e-37 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 138.46 E-value: 2.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 46 IFINNDWHESKSgrKFATYNPS-TLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRA 124
Cdd:TIGR01237 35 LVINGERVETEN--KIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEA---WKKTDPEERAAILFKAAAIVRRRRH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 125 ILATLETMDTGKPFLHAFfVDLEGCIKTFRYFAGWADKIQGR----TIPTDDNVVCFTrhePIGVCGAITPWNFPLLMLA 200
Cdd:TIGR01237 110 EFSALLVKEVGKPWNEAD-AEVAEAIDFMEYYARQMIELAKGkpvnSREGETNQYVYT---PTGVTVVISPWNFPFAIMV 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148675271 201 WKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:TIGR01237 186 GMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREV 258
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
65-276 |
6.20e-36 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 136.64 E-value: 6.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 65 NPSTLEKIC-EVEEGDKPDVDKAVEAAQAAfqrGSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAF- 142
Cdd:PRK11809 665 NPADPRDIVgYVREATPAEVEQALESAVNA---APIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIa 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 143 ----FVDLegciktFRYFAGwadkiQGRTIPTDDNvvcftrHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPA 218
Cdd:PRK11809 742 evreAVDF------LRYYAG-----QVRDDFDNDT------HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPA 804
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 148675271 219 EQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVSPL 276
Cdd:PRK11809 805 EQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARL 862
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
64-270 |
7.81e-36 |
|
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: 133.14 E-value: 7.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 64 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQ-LADLVERDRAILATLETMdTGKPFLHAf 142
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAA-QKG--WRAVPLEERKAIVTRaVELLAANTDEIAEELTWQ-MGRPIAQA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 143 fvdlEGCIKTF----RYFAGWADK-IQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKP 217
Cdd:cd07102 76 ----GGEIRGMleraRYMISIAEEaLADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKH 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 148675271 218 AEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTvGAAISSHPQINKIAFTGS 270
Cdd:cd07102 152 SPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGS 203
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
82-273 |
9.05e-35 |
|
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: 130.08 E-value: 9.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 82 DVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFF--------VDLEgcIKTF 153
Cdd:cd07095 1 QVDAAVAAARAAF---PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTevaamagkIDIS--IKAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 154 RYFAGwadkiqGRTIPTDdNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIK 233
Cdd:cd07095 76 HERTG------ERATPMA-QGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148675271 234 EVGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07095 149 EAGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAAT 187
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
47-270 |
2.63e-34 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 129.69 E-value: 2.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 47 FINNDWHESkSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRAIL 126
Cdd:PRK09457 4 WINGDWIAG-QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAF---PAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 127 ATLETMDTGKPFLHAffvdlegciKTfrYFAGWADKI-------QGRT----IPTDDNVVCFtRHEPIGVCGAITPWNFP 195
Cdd:PRK09457 80 AEVIARETGKPLWEA---------AT--EVTAMINKIaisiqayHERTgekrSEMADGAAVL-RHRPHGVVAVFGPYNFP 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148675271 196 LLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGS 270
Cdd:PRK09457 148 GHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGS 221
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
45-273 |
5.43e-34 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 128.85 E-value: 5.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 45 KIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFqrgSPWRRLDALSRGQLLHQLADLVERDRA 124
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF---LTWGQTSLAQRTSVLLRYQALLKEHRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 125 ILATLETMDTGKPFLHAFFvDLEGCIKTFRYFAGWADKIQGRTIPT-DDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKL 203
Cdd:TIGR01722 79 EIAELITAEHGKTHSDALG-DVARGLEVVEHACGVNSLLKGETSTQvATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 204 APALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGaAISSHPQINKIAFTGSTEV 273
Cdd:TIGR01722 158 PIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVD-RLLEHPDVKAVSFVGSTPI 226
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
45-269 |
4.70e-31 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 121.02 E-value: 4.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 45 KIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAfQRGspWRRLDALSRGQLLHQLADLVERDRA 124
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA-QKA--WAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 125 ILATLETMDTGKPFLHAFF-----VDL------EGCiktfRYFAgwadkiQGRTIPTDD------NVVCFTRHEPIGVCG 187
Cdd:PLN00412 94 PIAECLVKEIAKPAKDAVTevvrsGDLisytaeEGV----RILG------EGKFLVSDSfpgnerNKYCLTSKIPLGVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 188 AITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAF 267
Cdd:PLN00412 164 AIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISF 243
|
..
gi 148675271 268 TG 269
Cdd:PLN00412 244 TG 245
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
16-270 |
5.67e-30 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 118.70 E-value: 5.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 16 PFIPLLVPTCSLWASCAPLQRPLRTMK-KAKIFINNDWHESKSGRKFATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAF 94
Cdd:PLN02419 85 PLRPQFLALRSSWLSTSPEQSTQPQMPpRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 95 QRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTDDNV 174
Cdd:PLN02419 165 PL---WRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKT-LKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 175 V-CFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVG 253
Cdd:PLN02419 241 VdTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN 320
|
250
....*....|....*..
gi 148675271 254 aAISSHPQINKIAFTGS 270
Cdd:PLN02419 321 -AICDDEDIRAVSFVGS 336
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
62-270 |
1.40e-29 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 116.38 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 62 ATYNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPfLHA 141
Cdd:PRK09406 4 ATINPATGETVKTFTALTDDEVDAAIARAHARFRD---YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT-LAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 142 FFVDLEGCIKTFRYFAGWADKIQGRTiPTDDNVV----CFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKP 217
Cdd:PRK09406 80 AKAEALKCAKGFRYYAEHAEALLADE-PADAAAVgasrAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148675271 218 AEQTPLTALYLASLIKEVGFPPGVVNIVpgfgpTVGA----AISSHPQINKIAFTGS 270
Cdd:PRK09406 159 ASNVPQTALYLADLFRRAGFPDGCFQTL-----LVGSgaveAILRDPRVAAATLTGS 210
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
64-273 |
2.21e-29 |
|
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: 115.86 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 64 YNPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFF 143
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQRE---WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 144 vdleGCIKTFryfagwADKIQ-----G----RTIPTDDNVVCFTR-----HEPIGVCGAITPWNFPLLMLAWKLAPALCC 209
Cdd:cd07098 78 ----GEILVT------CEKIRwtlkhGekalRPESRPGGLLMFYKrarveYEPLGVVGAIVSWNYPFHNLLGPIIAALFA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148675271 210 GNTVVLKPAEQTPLTALYLASLIKEV----GFPPGVVNIVPGFGPTvGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07098 148 GNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPV 214
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
65-288 |
7.77e-27 |
|
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: 108.66 E-value: 7.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 65 NPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRGSPWrrLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfV 144
Cdd:cd07148 5 NPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK-V 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 145 DLEGCIKTFRYFAGWADKIQGRTIPTD-----DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAE 219
Cdd:cd07148 82 EVTRAIDGVELAADELGQLGGREIPMGltpasAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 220 QTPLTALYLASLIKEVGFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEVS-PLCELLAETTTCSI 288
Cdd:cd07148 162 ATPLSCLAFVDLLHEAGLPEGWCQAVPC-ENAVAEKLVTDPRVAFFSFIGSARVGwMLRSKLAPGTRCAL 230
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
71-273 |
4.09e-24 |
|
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: 101.51 E-value: 4.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 71 KICEVEEGDKPDVDKAVEAAQAAfqRGSpWRRLDALSRGQLLHQLADLVE---RDRAILATLetMDTGKPFLHAffvdlE 147
Cdd:cd07123 59 VLATYHYADAALVEKAIEAALEA--RKE-WARMPFEDRAAIFLKAADLLSgkyRYELNAATM--LGQGKNVWQA-----E 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 148 ---GC--IKTFRYFAGWADKI-QGRTIPTDDNVVCFTRHEPI-GVCGAITPWNFPLLMLAWKLAPALCcGNTVVLKPAEQ 220
Cdd:cd07123 129 idaACelIDFLRFNVKYAEELyAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDT 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 148675271 221 TPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07123 208 AVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPT 260
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
86-273 |
3.73e-23 |
|
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: 97.98 E-value: 3.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 86 AVEAAQAAFQRGS----PWRR--LDALSRGqllhqladLVERDRAILATLETmDTGKPFLHAFFVDLEGCIKTFRY---- 155
Cdd:cd07087 3 LVARLRETFLTGKtrslEWRKaqLKALKRM--------LTENEEEIAAALYA-DLGKPPAEAYLTEIAVVLGEIDHalkh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 156 FAGWADKiqgRTIPTDDNVV---CFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLI 232
Cdd:cd07087 74 LKKWMKP---RRVSVPLLLQpakAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148675271 233 KEVgFPPGVVNIVPGfGPTVGAAISSHPqINKIAFTGSTEV 273
Cdd:cd07087 151 PKY-FDPEAVAVVEG-GVEVATALLAEP-FDHIFFTGSPAV 188
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
47-273 |
4.81e-22 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 95.29 E-value: 4.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 47 FINNDWheSKSGRKFATYNPSTLEKICEVEEGDKPDVDkavEAAQAAFQRGSPWRRLDALSRGQLLHQLADLVERDRAIL 126
Cdd:PLN02315 24 YVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYE---EGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 127 ATLETMDTGKpFLHAFFVDLEGCIKTFRYFAGWADKIQGRTIPTD-DNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAP 205
Cdd:PLN02315 99 GRLVSLEMGK-ILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148675271 206 ALCCGNTVVLKPAEQTPLTALYLASLIKEV----GFPPGVVNIVPGfGPTVGAAISSHPQINKIAFTGSTEV 273
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKV 248
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
89-273 |
2.11e-21 |
|
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: 93.07 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 89 AAQAAFQRGSPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFLHAFfvDLEGCIKTFRYFA--GWADKIQGR 166
Cdd:cd07084 4 ALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAE--NICGDQVQLRARAfvIYSYRIPHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 167 TIPTDDNVVCFTRHE---PIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG-FPPGVV 242
Cdd:cd07084 82 PGNHLGQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDV 161
|
170 180 190
....*....|....*....|....*....|.
gi 148675271 243 NIVPGFGPTvGAAISSHPQINKIAFTGSTEV 273
Cdd:cd07084 162 TLINGDGKT-MQALLLHPNPKMVLFTGSSRV 191
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
82-273 |
4.58e-20 |
|
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: 89.20 E-value: 4.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 82 DVDKAVEAAQAAFQRGS----PWRRldalsrgQLLHQLADLVERDRAILATLETMDTGKPFLHAFFVDLEGCIKTFRYFA 157
Cdd:cd07135 6 EIDSIHSRLRATFRSGKtkdlEYRL-------WQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHML 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 158 G----WA-DKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLI 232
Cdd:cd07135 79 KnlkkWAkDEKVKDGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148675271 233 KEvGFPPGVVNIVPGFGPTVGAAISSHpqINKIAFTGSTEV 273
Cdd:cd07135 159 PK-YLDPDAFQVVQGGVPETTALLEQK--FDKIFYTGSGRV 196
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
179-273 |
1.64e-19 |
|
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: 87.54 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 179 RHEPIGVCGAITPWNFPlLMLAwkLAP---ALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGfGPTVGAA 255
Cdd:cd07133 98 EYQPLGVVGIIVPWNYP-LYLA--LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTG-GADVAAA 172
|
90
....*....|....*...
gi 148675271 256 ISSHPqINKIAFTGSTEV 273
Cdd:cd07133 173 FSSLP-FDHLLFTGSTAV 189
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
176-273 |
3.86e-19 |
|
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: 86.51 E-value: 3.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 176 CFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGfGPTVGAA 255
Cdd:cd07134 94 SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-DAEVAQA 171
|
90
....*....|....*...
gi 148675271 256 ISSHPqINKIAFTGSTEV 273
Cdd:cd07134 172 LLELP-FDHIFFTGSPAV 188
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
81-273 |
4.59e-17 |
|
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: 80.53 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 81 PDVDKAVEAAQAAFQRGSPWRRldalsrgQLLHQLADLV-ERDRAILATLETmDTGKPFLHAFF----VDLEGCIKTFRY 155
Cdd:cd07137 3 RLVRELRETFRSGRTRSAEWRK-------SQLKGLLRLVdENEDDIFAALRQ-DLGKPSAESFRdevsVLVSSCKLAIKE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 156 FAGWAD----KIQGRTIPTDDNVVCftrhEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASL 231
Cdd:cd07137 75 LKKWMApekvKTPLTTFPAKAEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 148675271 232 IKEVgFPPGVVNIVPGfGPTVGAAISSHpQINKIAFTGSTEV 273
Cdd:cd07137 151 IPEY-LDTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRV 189
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
181-273 |
6.95e-16 |
|
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: 77.16 E-value: 6.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 181 EPIGVCGAITPWNFPLLMLawkLAP---ALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGfGPTVGAAIS 257
Cdd:cd07136 99 EPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEENQELL 173
|
90
....*....|....*.
gi 148675271 258 SHPqINKIAFTGSTEV 273
Cdd:cd07136 174 DQK-FDYIFFTGSVRV 188
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
176-276 |
7.48e-16 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 77.38 E-value: 7.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 176 CFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGfGPTVGAA 255
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTE 180
|
90 100
....*....|....*....|.
gi 148675271 256 ISSHPqINKIAFTGSTEVSPL 276
Cdd:PTZ00381 181 LLKEP-FDHIFFTGSPRVGKL 200
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
85-232 |
5.57e-14 |
|
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: 71.48 E-value: 5.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 85 KAVEAAQAAFQRGspwRRLDALSRGQLLHQLADLV-ERDRAILATLEtMDTGKPFLHAFFVDLEGCIKTFRY----FAGW 159
Cdd:cd07132 2 EAVRRAREAFSSG---KTRPLEFRIQQLEALLRMLeENEDEIVEALA-KDLRKPKFEAVLSEILLVKNEIKYaisnLPEW 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148675271 160 A-DKIQGRTIPT--DDnvvCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLI 232
Cdd:cd07132 78 MkPEPVKKNLATllDD---VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELI 150
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
65-270 |
7.11e-14 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 71.43 E-value: 7.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 65 NPSTLEKICEVEEGDKPDVDKAVEAAQAAFQRgspWRRLDALSRGQLLHQLADLVeRDRAI-LATLETMDTGKPFLHAff 143
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRD---WRETNIDYRAQKLRDIGKAL-RARSEeMAQMITREMGKPINQA-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 144 vdlEGCIKTFRYFAGWADKiQG----RTIPT-DDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPA 218
Cdd:PRK13968 87 ---RAEVAKSANLCDWYAE-HGpamlKAEPTlVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 148675271 219 EQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAISShPQINKIAFTGS 270
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGS 213
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
83-271 |
6.91e-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: 68.34 E-value: 6.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 83 VDKAVEAAQAAFQrgsPWRRLDALSRGQLLHQLADLVERDRAILATLETMDTGKPFlhaffVDLEGCI-KT---FRYFA- 157
Cdd:cd07129 1 VDAAAAAAAAAFE---SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPE-----ARLQGELgRTtgqLRLFAd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 158 -----GWADKI------QGRTIPTDDNVVCFTRHEPIGVCGAItpwNFPLlmlAWKL-----APALCCGNTVVLKPAEQT 221
Cdd:cd07129 73 lvregSWLDARidpadpDRQPLPRPDLRRMLVPLGPVAVFGAS---NFPL---AFSVaggdtASALAAGCPVVVKAHPAH 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 148675271 222 PLTALYLASLIKEV----GFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGST 271
Cdd:cd07129 147 PGTSELVARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSR 200
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
41-272 |
3.47e-12 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 66.27 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 41 MKKAKIFINNDWHESkSGRKFATYNPSTLEKICEVeegDKPDVDKAVEAAQAAFQRGSPWRRLDALSRGQLLHQLADLVE 120
Cdd:PRK11903 2 TELLANYVAGRWQAG-SGAGTPLFDPVTGEELVRV---SATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 121 RDRAILATLETMDTGKPFLHAFFvDLEGCIKTFRYFAGWADKIQGRTIPTDDNVVCFTRHEPI----------GVCGAIT 190
Cdd:PRK11903 78 ANRDAYYDIATANSGTTRNDSAV-DIDGGIFTLGYYAKLGAALGDARLLRDGEAVQLGKDPAFqgqhvlvptrGVALFIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 191 PWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG-FPPGVVNIVPGfgptVGAAISSHPQ-INKIAFT 268
Cdd:PRK11903 157 AFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG----SSAGLLDHLQpFDVVSFT 232
|
....
gi 148675271 269 GSTE 272
Cdd:PRK11903 233 GSAE 236
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
181-273 |
3.99e-11 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 63.21 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 181 EPIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGfGPTVGAAISSHP 260
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKY-LDSKAVKVIEG-GPAVGEQLLQHK 184
|
90
....*....|...
gi 148675271 261 QiNKIAFTGSTEV 273
Cdd:PLN02203 185 W-DKIFFTGSPRV 196
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
133-273 |
7.52e-10 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 59.29 E-value: 7.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 133 DTGKPFLHAFFVD---LEGCIK-TFRYFAGWADKIQGRTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLAWKLAPALC 208
Cdd:PLN02174 59 DLGKPELESSVYEvslLRNSIKlALKQLKNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAIS 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148675271 209 CGNTVVLKPAEQTPLTALYLASLIKEVgFPPGVVNIVPGFGPTVGAAISShpQINKIAFTGSTEV 273
Cdd:PLN02174 139 AGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALLEQ--KWDKIFYTGSSKI 200
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
108-273 |
9.81e-10 |
|
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: 58.77 E-value: 9.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 108 RGQLLHQLADLVERDRAILATLETMDTGKPF--LHAFFVDLEGCIK--------TFRYFAGWADKIQGRTIPtdDNVVCF 177
Cdd:cd07077 18 RDLIINAIANALYDTRQRLASEAVSERGAYIrsLIANWIAMMGCSEsklyknidTERGITASVGHIQDVLLP--DNGETY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 178 TRHEPIGVCGAITPWNFPLLMLAwKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEV---GFPPGVVNIVPGFGPTVGA 254
Cdd:cd07077 96 VRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPHPSDELAE 174
|
170
....*....|....*....
gi 148675271 255 AISSHPQINKIAFTGSTEV 273
Cdd:cd07077 175 ELLSHPKIDLIVATGGRDA 193
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
47-247 |
1.98e-08 |
|
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: 54.97 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 47 FINNDWHESkSGRKFATYNPSTLEKICEVEeGDKPDVDKAVEAAQaafQRGSP-WRRLDALSRGQLLHQLAD-LVERDRA 124
Cdd:cd07128 4 YVAGQWHAG-TGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYAR---EKGGPaLRALTFHERAAMLKALAKyLMERKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 125 ILATleTMDTGKPFLHAFfVDLEGCIKTFRYFAGwadkiQGRTIPTDDNV-------------------VCFTRHepiGV 185
Cdd:cd07128 79 LYAL--SAATGATRRDSW-IDIDGGIGTLFAYAS-----LGRRELPNAHFlvegdveplskdgtfvgqhILTPRR---GV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148675271 186 CGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVG-FPPGVVNIVPG 247
Cdd:cd07128 148 AVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG 210
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
182-274 |
2.86e-06 |
|
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: 48.26 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 182 PIGVCGAITPWNFPLLMLAWKLAPALCCGNTVVLKPAEQTPLTALYLASLIKEVGFPPGVVNIVPGFGPTVGAAIS-SHP 260
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLeANP 221
|
90
....*....|....
gi 148675271 261 QInkIAFTGSTEVS 274
Cdd:cd07126 222 RM--TLFTGSSKVA 233
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
79-271 |
6.16e-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: 40.92 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 79 DKPDVDKAVEAAQAAFQRgspWRRLDALSR-GQLLHQLADLVERDRAIL-ATLETmdTGKPFLHAFFVD----LEGCIKT 152
Cdd:cd07127 82 PQCDPDALLAAARAAMPG---WRDAGARARaGVCLEILQRLNARSFEMAhAVMHT--TGQAFMMAFQAGgphaQDRGLEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148675271 153 FRYfagwADKIQGRTIPTDDNVVCFTRHEPI-----------GV-----CGAITPWN-FPLLMlawklaPALCCGNTVVL 215
Cdd:cd07127 157 VAY----AWREMSRIPPTAEWEKPQGKHDPLamektftvvprGValvigCSTFPTWNgYPGLF------ASLATGNPVIV 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148675271 216 KPAeqtPLTALYLASLIK-------EVGFPPGVVNIV---PGFGptVGAAISSHPQINKIAFTGST 271
Cdd:cd07127 227 KPH---PAAILPLAITVQvarevlaEAGFDPNLVTLAadtPEEP--IAQTLATRPEVRIIDFTGSN 287
|
|
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