|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
34-240 |
4.59e-133 |
|
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: 382.72 E-value: 4.59e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 34 GDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSGVWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPI 113
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 114 SDSLNIDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPS 193
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2585406586 194 EKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVDTL 240
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDAL 207
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
9-240 |
6.62e-113 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 332.63 E-value: 6.62e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 9 WEQRAKALKIEGRAYINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSGVWSRLAPAKRKTVMI 88
Cdd:PRK09847 9 WQDKALSLAIENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 89 RFAALLKANAEELALLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWN 168
Cdd:PRK09847 89 KLADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWN 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2585406586 169 FPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVDTL 240
Cdd:PRK09847 169 FPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAI 240
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
19-238 |
1.67e-93 |
|
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: 282.40 E-value: 1.67e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 19 EGRAYINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFnsGVWSRLAPAKRKTVMIRFAALLKANA 98
Cdd:COG1012 5 EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 99 EELALLETLDMGKPISDSLnIDVPGAAQALSWSGEAIDKIYDEVAATP-HDQLGLVTREPVGVVGAIVPWNFPLMMACWK 177
Cdd:COG1012 83 EELAALLTLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2585406586 178 LGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVD 222
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
33-238 |
7.18e-84 |
|
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: 257.07 E-value: 7.18e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 33 SGDTFECISPVDGRLLATVASCDASDAQCAVENARATFnsGVWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKP 112
Cdd:pfam00171 5 ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAF--PAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 113 ISDSLnIDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKP 192
Cdd:pfam00171 83 LAEAR-GEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2585406586 193 SEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:pfam00171 162 SELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVR 207
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
23-238 |
2.81e-83 |
|
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: 255.98 E-value: 2.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSGVWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:cd07091 7 FINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPAL 182
Cdd:cd07091 87 ALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPAL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2585406586 183 STGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07091 167 AAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVD 222
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
23-238 |
1.78e-78 |
|
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: 244.14 E-value: 1.78e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSGVWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSlNIDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPAL 182
Cdd:cd07119 81 RLETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2585406586 183 STGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVD 215
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
23-238 |
1.96e-75 |
|
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: 235.85 E-value: 1.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSGVWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPAL 182
Cdd:cd07142 87 ALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPAL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2585406586 183 STGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07142 167 ACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVD 222
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
41-238 |
8.08e-75 |
|
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: 233.87 E-value: 8.08e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 41 SPVDGRLLATVASCDASDAQCAVENARATFNsgVWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLNID 120
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFE--AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 121 VPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTA 200
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSA 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 2585406586 201 IRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07115 161 LRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVD 198
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
23-238 |
2.33e-71 |
|
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: 225.69 E-value: 2.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSG-VWSRLAPAKRKTVMIRFAALLKANAEEL 101
Cdd:cd07141 10 FINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGsPWRTMDASERGRLLNKLADLIERDRAYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 102 ALLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPA 181
Cdd:cd07141 90 ASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2585406586 182 LSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07141 170 LACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDID 226
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
23-238 |
1.20e-70 |
|
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: 223.82 E-value: 1.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSgVWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:cd07144 11 FINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFES-WWSKVTGEERGELLDKLADLVEKNRDLLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPAL 182
Cdd:cd07144 90 AIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2585406586 183 STGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07144 170 AAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVD 225
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
23-238 |
3.01e-70 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 223.16 E-value: 3.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSGVWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:PLN02766 24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPAL 182
Cdd:PLN02766 104 ALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPAL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2585406586 183 STGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:PLN02766 184 AAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVD 239
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
40-238 |
3.76e-69 |
|
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: 219.34 E-value: 3.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 40 ISPVDGRLLATVASCDASDAQCAVENARATFNSGVWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLNi 119
Cdd:cd07114 2 INPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 120 DVPGAAQALSWSGEAIDKIYDEVAATPH-DQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPL 198
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKgDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2585406586 199 TAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVA 200
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
40-238 |
4.35e-69 |
|
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: 218.97 E-value: 4.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 40 ISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLNI 119
Cdd:cd07093 2 FNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG--WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 120 DVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLT 199
Cdd:cd07093 80 DIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 2585406586 200 AIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVD 198
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
24-240 |
8.07e-69 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 220.45 E-value: 8.07e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 24 INGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSGVWSRLAPAKRKTVMIRFAALLKANAEELAL 103
Cdd:PLN02466 62 INGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHNDELAA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 104 LETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKIYDEV--AATPHDQLGLvtREPVGVVGAIVPWNFPLMMACWKLGPA 181
Cdd:PLN02466 142 LETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTvpADGPHHVQTL--HEPIGVAGQIIPWNFPLLMFAWKVGPA 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2585406586 182 LSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVDTL 240
Cdd:PLN02466 220 LACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKL 278
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
62-238 |
1.16e-67 |
|
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: 214.76 E-value: 1.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 62 AVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLnIDVPGAAQALSWSGEAIDKIYDE 141
Cdd:cd07078 3 AVAAARAAFKA--WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEAL-GEVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 142 VAATPH-DQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVL 220
Cdd:cd07078 80 VIPSPDpGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVV 159
|
170
....*....|....*...
gi 2585406586 221 PGYGHTVGNALAVHMDVD 238
Cdd:cd07078 160 TGDGDEVGAALASHPRVD 177
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
23-238 |
1.68e-67 |
|
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: 215.86 E-value: 1.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSGVWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:cd07143 10 FINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGLKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPAL 182
Cdd:cd07143 90 SIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2585406586 183 STGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07143 170 AAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDID 225
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
23-240 |
1.29e-66 |
|
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: 213.36 E-value: 1.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPAL 182
Cdd:cd07559 82 VAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPAL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2585406586 183 STGNSVILKPSEKSPLTAIRIAALaVEAGIPKGVFNVLPGYGHTVGNALAVHMDVDTL 240
Cdd:cd07559 162 AAGNTVVLKPASQTPLSILVLMEL-IGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKL 218
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
40-241 |
3.63e-66 |
|
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: 211.32 E-value: 3.63e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 40 ISPVDGRLLATVASCDASDAQCAVENARATFNSGvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLNi 119
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESG-WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 120 DVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLT 199
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2585406586 200 AIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVDTLV 241
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHIS 201
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
23-238 |
1.39e-65 |
|
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: 210.51 E-value: 1.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSGVWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKI-YDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPA 181
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFpFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2585406586 182 LSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGyGHTVGNALAVHMDVD 238
Cdd:cd07139 162 LAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVD 217
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
40-231 |
6.09e-64 |
|
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: 205.36 E-value: 6.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 40 ISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLnI 119
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT--WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR-G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 120 DVPGAAQALSWSGEAIDKIYDEVAATPH-DQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPL 198
Cdd:cd07103 79 EVDYAASFLEWFAEEARRIYGRTIPSPApGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPL 158
|
170 180 190
....*....|....*....|....*....|...
gi 2585406586 199 TAIRIAALAVEAGIPKGVFNVLPGYGHTVGNAL 231
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGSPAEIGEAL 191
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
23-238 |
3.58e-62 |
|
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: 201.58 E-value: 3.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFnsGVWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPAL 182
Cdd:TIGR01804 79 KLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPAL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2585406586 183 STGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:TIGR01804 159 AAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVA 214
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
23-238 |
1.51e-61 |
|
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: 199.65 E-value: 1.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:cd07138 2 YIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA--WSATSVEERAALLERIAEAYEARADELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKI-YDEVAATphdqlGLVTREPVGVVGAIVPWNFPLMMACWKLGPA 181
Cdd:cd07138 80 QAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFeFEERRGN-----SLVVREPIGVCGLITPWNWPLNQIVLKVAPA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2585406586 182 LSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07138 155 LAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVD 211
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
21-238 |
1.65e-61 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 200.11 E-value: 1.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 21 RAYINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFnsGVWSRLAPAKRKTVMIRFAALLKANAEE 100
Cdd:PRK13252 8 SLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQ--KIWAAMTAMERSRILRRAVDILRERNDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 101 LALLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGP 180
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2585406586 181 ALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGhTVGNALAVHMDVD 238
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIA 222
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
23-238 |
3.18e-61 |
|
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: 199.03 E-value: 3.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA--WERLPAIERAAYLRKLADLIRENADELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSlNIDVPGAAQALSWSGEAIDKIYDEVAA--TPHDQLgLVTREPVGVVGAIVPWNFPLMMACWKLGP 180
Cdd:cd07088 79 KLIVEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIIPsdRPNENI-FIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2585406586 181 ALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVG 214
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
66-238 |
3.31e-61 |
|
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: 196.30 E-value: 3.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 66 ARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLnIDVPGAAQALSWSGEAIDKIYDEVAAT 145
Cdd:cd06534 3 ARAAFKA--WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGPELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 146 PHDQ-LGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYG 224
Cdd:cd06534 80 PDPGgEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGG 159
|
170
....*....|....
gi 2585406586 225 HTVGNALAVHMDVD 238
Cdd:cd06534 160 DEVGAALLSHPRVD 173
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
23-238 |
1.38e-60 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 197.44 E-value: 1.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAvSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:PRK13473 6 LINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE--WSQTTPKERAEALLKLADAIEENADEFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSLNIDVP----------GAAQAL--SWSGEaidkiYDEvaatphDQLGLVTREPVGVVGAIVPWNFP 170
Cdd:PRK13473 83 RLESLNCGKPLHLALNDEIPaivdvfrffaGAARCLegKAAGE-----YLE------GHTSMIRRDPVGVVASIAPWNYP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2585406586 171 LMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAgIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:PRK13473 152 LMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVR 218
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
16-237 |
1.38e-60 |
|
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: 197.72 E-value: 1.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 16 LKIEGRAYINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSGVWSRLAPAKRKTVMIRFAALLK 95
Cdd:cd07140 2 LKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLME 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 96 ANAEELALLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKIYDEV----AATPHDQLGLVTREPVGVVGAIVPWNFPL 171
Cdd:cd07140 82 EHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTipinQARPNRNLTLTKREPIGVCGIVIPWNYPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2585406586 172 MMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDV 237
Cdd:cd07140 162 MMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDV 227
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
23-240 |
3.57e-60 |
|
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: 196.52 E-value: 3.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPAL 182
Cdd:cd07117 82 MVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPAL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2585406586 183 STGNSVILKPSEKSPLTAIRIAALaVEAGIPKGVFNVLPGYGHTVGNALAVHMDVDTL 240
Cdd:cd07117 162 AAGNTVVIKPSSTTSLSLLELAKI-IQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKL 218
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
40-238 |
3.76e-59 |
|
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: 193.32 E-value: 3.76e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 40 ISPVDGRLLATVASCDASDAQCAVENARATFNSGVWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLNi 119
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 120 DVPGAA--------QALSWSGEAIDKIYDevaatphDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILK 191
Cdd:cd07118 81 EIEGAAdlwryaasLARTLHGDSYNNLGD-------DMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2585406586 192 PSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07118 154 PSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVD 200
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
23-238 |
1.26e-57 |
|
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: 189.91 E-value: 1.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRLFA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKIYDEVAAtphdqlglvtREPVGVVGAIVPWNFPLMMACWKLGPAL 182
Cdd:cd07111 103 VLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLDTELAG----------WKPVGVVGQIVPWNFPLLMLAWKICPAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2585406586 183 STGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTvGNALAVHMDVD 238
Cdd:cd07111 173 AMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVD 227
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
23-237 |
5.00e-55 |
|
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: 183.03 E-value: 5.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSGVWSRLaPAKRKTVMIRFAALLKANAEELA 102
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSAWAKTT-PAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKIYDEVAAT--PHDQ----LGLVTREPVGVVGAIVPWNFPLMMACW 176
Cdd:cd07113 82 QLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPsiPSMQgeryTAFTRREPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2585406586 177 KLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHtVGNALAVHMDV 237
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDV 221
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
11-231 |
9.96e-55 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 182.58 E-value: 9.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 11 QRAKALKIEGraYINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRF 90
Cdd:PLN02278 18 RNAGLLRTQG--LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPS--WSKLTASERSKILRRW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 91 AALLKANAEELALLETLDMGKPISDSLNiDVPGAAQALSWSGEAIDKIYDEVAATPH-DQLGLVTREPVGVVGAIVPWNF 169
Cdd:PLN02278 94 YDLIIANKEDLAQLMTLEQGKPLKEAIG-EVAYGASFLEYFAEEAKRVYGDIIPSPFpDRRLLVLKQPVGVVGAITPWNF 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2585406586 170 PLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNAL 231
Cdd:PLN02278 173 PLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDAL 234
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
40-238 |
1.37e-54 |
|
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: 181.29 E-value: 1.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 40 ISPVDGRLLATVASCDASDAQCAVENARATFNSGVWSRlAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLNI 119
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWST-DAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 120 DVPGAAQALSWSGEAIDKIYDEVAATPHDQLG-----LVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSE 194
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVPALRGgpgrrVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2585406586 195 KSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVD 204
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
23-239 |
1.00e-53 |
|
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: 179.85 E-value: 1.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGR-LLATVASCDASDAQCAVENARATFnsGVWSRLAPAKRKTVMIRFAALLKANAEEL 101
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEeVVGTFPLSTASDVDAAVEAAREAF--PEWRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 102 ALLETLDMGKPISDSLNiDVPGAAQALSWSGEAIDKIYDEVaaTPH---DQLGLVTREPVGVVGAIVPWNFPLMMACWKL 178
Cdd:cd07131 80 ARLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGET--VPSelpNKDAMTRRQPIGVVALITPWNFPVAIPSWKI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2585406586 179 GPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVDT 239
Cdd:cd07131 157 FPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDV 217
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
23-238 |
2.12e-53 |
|
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: 178.86 E-value: 2.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:cd07085 4 FINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA--WSATPVLKRQQVMFKFRQLLEENLDELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSL--------NIDVPGAAQALSwSGEaidkiYDEVAATPHDQLglVTREPVGVVGAIVPWNFPLMMA 174
Cdd:cd07085 82 RLITLEHGKTLADARgdvlrgleVVEFACSIPHLL-KGE-----YLENVARGIDTY--SYRQPLGVVAGITPFNFPAMIP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2585406586 175 CWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGyGHTVGNALAVHMDVD 238
Cdd:cd07085 154 LWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIK 216
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
23-237 |
1.70e-52 |
|
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: 176.49 E-value: 1.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA--WGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPAL 182
Cdd:cd07116 82 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPAL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2585406586 183 STGNSVILKPSEKSPLTAIRIAALAVEAgIPKGVFNVLPGYGHTVGNALAVHMDV 237
Cdd:cd07116 162 AAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRI 215
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
40-237 |
2.22e-52 |
|
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: 175.57 E-value: 2.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 40 ISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLnI 119
Cdd:cd07090 2 IEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE--WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR-V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 120 DVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLT 199
Cdd:cd07090 79 DIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLT 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 2585406586 200 AIRIAALAVEAGIPKGVFNVLPGYGHTvGNALAVHMDV 237
Cdd:cd07090 159 ALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDV 195
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
21-238 |
1.32e-51 |
|
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: 173.97 E-value: 1.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 21 RAYINGEYTAavSGDTFECISPVDGR-LLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAE 99
Cdd:cd07097 2 RNYIDGEWVA--GGDGEENRNPSDTSdVVGKYARASAEDADAAIAAAAAAFPA--WRRTSPEARADILDKAGDELEARKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 100 ELALLETLDMGKPISDSLNiDVPGAAQALSW-SGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKL 178
Cdd:cd07097 78 ELARLLTREEGKTLPEARG-EVTRAGQIFRYyAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 179 GPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07097 157 APALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVD 216
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
40-238 |
1.53e-51 |
|
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: 173.28 E-value: 1.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 40 ISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLNI 119
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPS--WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 120 DVPGAAQALSWSGEAIdKIYDEVAATPH--DQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSP 197
Cdd:cd07092 80 ELPGAVDNFRFFAGAA-RTLEGPAAGEYlpGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2585406586 198 LTAIRIAALAVEaGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07092 159 LTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVR 198
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
23-238 |
7.61e-51 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 172.61 E-value: 7.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATF---NSGVWSRLAPAKRKTVMIRFAALLKANAE 99
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnKGKDWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 100 ELALLETLDMGKPISDSL--NIDVPGAAQALSWSGEAIDKIYDEVAATPHDQL-GLVTREPVGVVGAIVPWNFPLMMACW 176
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAwdMDDVAGCFEYYADLAEALDAKQKAPVSLPMETFkGYVLKEPLGVVGLITPWNYPLLMATW 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2585406586 177 KLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:PLN02467 171 KVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVD 232
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
37-237 |
1.34e-50 |
|
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: 170.85 E-value: 1.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 37 FECISPVDGRLLATVASCDASDAQCAVENARATFNSGvwSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDS 116
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM--KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 117 LNiDVPGAAQALSWSGEAIDKIYDEV-----AATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILK 191
Cdd:cd07149 79 RK-EVDRAIETLRLSAEEAKRLAGETipfdaSPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2585406586 192 PSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDV 237
Cdd:cd07149 158 PASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRV 203
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
40-238 |
2.18e-50 |
|
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: 170.02 E-value: 2.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 40 ISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSlNI 119
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG--WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-QF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 120 DVPGAAQalsWSGE-AIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPL 198
Cdd:cd07106 79 EVGGAVA---WLRYtASLDLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2585406586 199 TAIRIAALAVEAgIPKGVFNVLPGyGHTVGNALAVHMDVD 238
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIR 193
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
40-240 |
4.58e-50 |
|
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: 169.45 E-value: 4.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 40 ISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLnI 119
Cdd:cd07110 2 INPATEATIGEIPAATAEDVDAAVRAARRAFPR--WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAA-W 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 120 DVPGAAQALSWSG---EAIDKIYDEVAATPHDQL-GLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEK 195
Cdd:cd07110 79 DVDDVAGCFEYYAdlaEQLDAKAERAVPLPSEDFkARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2585406586 196 SPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVDTL 240
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKI 203
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
37-238 |
1.77e-49 |
|
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: 167.91 E-value: 1.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 37 FECISPVDGRLLATVASCDASDAQCAVENARATFNsgVWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDS 116
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKD--VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 117 lNIDVPGAAQALSWSGEAIDKIYDE---VAATPHDQLGLV--TREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILK 191
Cdd:cd07145 79 -RVEVERTIRLFKLAAEEAKVLRGEtipVDAYEYNERRIAftVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2585406586 192 PSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07145 158 PSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVN 204
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
38-240 |
5.19e-49 |
|
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: 166.84 E-value: 5.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 38 ECISPVDGRLLATVASCDASDAQCAVENARATFNsgVWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSL 117
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAE--NRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 118 nIDVPGAAQALSWSGEAIDKIYDEV-----AATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKP 192
Cdd:cd07094 80 -VEVDRAIDTLRLAAEEAERIRGEEipldaTQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2585406586 193 SEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVDTL 240
Cdd:cd07094 159 ASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAML 206
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
40-238 |
2.21e-46 |
|
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: 159.85 E-value: 2.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 40 ISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLNi 119
Cdd:cd07107 2 INPATGQVLARVPAASAADVDRAVAAARAAFPE--WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 120 DVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLT 199
Cdd:cd07107 79 DVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 2585406586 200 AIRIAALAVEAgIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07107 159 ALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVK 196
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
40-240 |
1.16e-45 |
|
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: 157.91 E-value: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 40 ISPVDGRLLATVASCDASDAQCAVENARATFnsGVWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLNI 119
Cdd:cd07108 2 INPATGQVIGEVPRSRAADVDRAVAAAKAAF--PEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 120 DVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLT 199
Cdd:cd07108 80 EAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2585406586 200 AIRIAALAVEAgIPKGVFNVLPGYGHTVGNALAVHMDVDTL 240
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKV 199
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
22-238 |
1.24e-42 |
|
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: 150.41 E-value: 1.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 22 AYINGEYTAAvSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNsGVWSRLAPAKRKTVMIRFAALLKANAEEL 101
Cdd:cd07082 4 YLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGR-GWWPTMPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 102 ALLETLDMGKPISDSLnIDVPGAAQALSWSGEAIDKIYDEVA---ATPHDQ--LGLVTREPVGVVGAIVPWNFPLMMACW 176
Cdd:cd07082 82 ANLLMWEIGKTLKDAL-KEVDRTIDYIRDTIEELKRLDGDSLpgdWFPGTKgkIAQVRREPLGVVLAIGPFNYPLNLTVS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2585406586 177 KLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07082 161 KLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRID 222
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
20-238 |
2.17e-42 |
|
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: 150.45 E-value: 2.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 20 GRAY---INGEytAAVSGDTFECISPVD-GRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLK 95
Cdd:cd07124 30 GREYplvIGGK--EVRTEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPT--WRRTPPEERARLLLRAAALLR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 96 ANAEELALLETLDMGKPISDSLNiDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMAC 175
Cdd:cd07124 106 RRRFELAAWMVLEVGKNWAEADA-DVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2585406586 176 WKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07124 185 GMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVR 247
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
23-240 |
1.34e-40 |
|
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: 145.01 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAvSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFnsGVWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAF--KEWRKVPAPRRGEIVRQIGEALRKKKEALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSLnidvpGAAQalswsgEAID----------KIYDEVAAT--P-HDQLglVTREPVGVVGAIVPWNF 169
Cdd:cd07086 79 RLVSLEMGKILPEGL-----GEVQ------EMIDicdyavglsrMLYGLTIPSerPgHRLM--EQWNPLGVVGVITAFNF 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2585406586 170 PLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEA----GIPKGVFNVLPGYGhTVGNALAVHMDVDTL 240
Cdd:cd07086 146 PVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGG-DGGELLVHDPRVPLV 219
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
21-231 |
1.70e-40 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 144.66 E-value: 1.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 21 RAYINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEE 100
Cdd:PRK11241 12 QALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPA--WRALTAKERANILRRWFNLMMEHQDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 101 LALLETLDMGKPISDSLNiDVPGAAQALSWSGEAIDKIY-DEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLG 179
Cdd:PRK11241 90 LARLMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYgDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAG 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2585406586 180 PALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNAL 231
Cdd:PRK11241 169 PALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGEL 220
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
37-238 |
7.02e-40 |
|
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: 142.47 E-value: 7.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 37 FECISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKP---- 112
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPA--WAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTygka 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 113 ---ISDSLNIDVPGAAQALSWSGEAIdkiydevaatPHDQLGLVT---REPVGVVGAIVPWNFPLMMACWKLGPALSTGN 186
Cdd:cd07150 79 wfeTTFTPELLRAAAGECRRVRGETL----------PSDSPGTVSmsvRRPLGVVAGITPFNYPLILATKKVAFALAAGN 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2585406586 187 SVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07150 149 TVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVR 200
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
42-238 |
2.28e-38 |
|
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: 138.65 E-value: 2.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 42 PVDGRLLATVASCDASDAQCAVENARATFnsgvwSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSL---- 117
Cdd:cd07146 6 PYTGEVVGTVPAGTEEALREALALAASYR-----STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRyevg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 118 ---NIDVPGAAQALSWSGEAIDKiydEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSE 194
Cdd:cd07146 81 raaDVLRFAAAEALRDDGESFSC---DLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2585406586 195 KSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVD 201
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
37-221 |
7.57e-38 |
|
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: 136.99 E-value: 7.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 37 FECISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDS 116
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRP--MRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 117 lNIDVPGAAQALSWSGEAIDKIYDEV-----AATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILK 191
Cdd:cd07147 79 -RGEVARAIDTFRIAAEEATRIYGEVlpldiSARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLK 157
|
170 180 190
....*....|....*....|....*....|
gi 2585406586 192 PSEKSPLTAIRIAALAVEAGIPKGVFNVLP 221
Cdd:cd07147 158 PASRTPLSALILGEVLAETGLPKGAFSVLP 187
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
40-240 |
9.77e-38 |
|
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: 136.70 E-value: 9.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 40 ISPVDGRLLATVASCDASDAQCAVENARATFNSGVWSRlAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSlNI 119
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEA-RF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 120 DVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLT 199
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2585406586 200 AIRIAALAVEA-GIPKGVFNVLPGYGHTVGNALAVHMDVDTL 240
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVI 201
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
40-232 |
5.67e-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: 131.98 E-value: 5.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 40 ISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSlni 119
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG--WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 120 dvPGAAQALSWSGEAIDKIYDEVAAT----PHDQL-GLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSE 194
Cdd:cd07102 76 --GGEIRGMLERARYMISIAEEALADirvpEKDGFeRYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSP 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 2585406586 195 KSPLTAIRIAALAVEAGIPKGVFNVLPGyGHTVGNALA 232
Cdd:cd07102 154 QTPLCGERFAAAFAEAGLPEGVFQVLHL-SHETSAALI 190
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
6-238 |
5.79e-36 |
|
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: 133.09 E-value: 5.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 6 RADWEQRAKALK----IEGRAY--INGEytAAVSGDTFECISPVDG-RLLATVASCDASDAQCAVENARATFNSgvWSRL 78
Cdd:cd07125 13 EVPLEALADALKafdeKEWEAIpiINGE--ETETGEGAPVIDPADHeRTIGEVSLADAEDVDAALAIAAAAFAG--WSAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 79 APAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLNiDVpgaaqalswsGEAID-----------KIYDEVAATPH 147
Cdd:cd07125 89 PVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADA-EV----------REAIDfcryyaaqareLFSDPELPGPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 148 DQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTV 227
Cdd:cd07125 158 GELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEI 237
|
250
....*....|.
gi 2585406586 228 GNALAVHMDVD 238
Cdd:cd07125 238 GEALVAHPRID 248
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
30-236 |
5.90e-36 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 133.08 E-value: 5.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 30 AAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATfnSGVWSRLAPAKRKTVMIRFAALLKANAEELALLETLDM 109
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA--QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 110 GKPISDSLN--IDVPGAAQALSWSGEAIDKiydevaatPHDQLGL--------VTREPVGVVGAIVPWNFPLMMACWKLG 179
Cdd:PRK09407 105 GKARRHAFEevLDVALTARYYARRAPKLLA--------PRRRAGAlpvltkttELRQPKGVVGVISPWNYPLTLAVSDAI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2585406586 180 PALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMD 236
Cdd:PRK09407 177 PALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDNAD 233
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
58-238 |
2.50e-34 |
|
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: 127.26 E-value: 2.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 58 DAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLetldmgkpisdslNIDVPGAAQALSWS--GEAI 135
Cdd:cd07104 1 DVDRAYAAAAAAQKA--WAATPPQERAAILRKAAEILEERRDEIADW-------------LIRESGSTRPKAAFevGAAI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 136 dKIYDEVAATPH------------DQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLT-AIR 202
Cdd:cd07104 66 -AILREAAGLPRrpegeilpsdvpGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLL 144
|
170 180 190
....*....|....*....|....*....|....*.
gi 2585406586 203 IAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:cd07104 145 IAEIFEEAGLPKGVLNVVPGGGSEIGDALVEHPRVR 180
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
40-231 |
4.08e-34 |
|
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: 126.95 E-value: 4.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 40 ISPVDGRLLATVASCDASDAQCAVENARATfnSGVWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLnI 119
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAA--QRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG-L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 120 DVPGAAQALSWSGEAIDKIYDEVAATPH----DQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEK 195
Cdd:cd07099 78 EVLLALEAIDWAARNAPRVLAPRKVPTGllmpNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEV 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 2585406586 196 SPLTAIRIAALAVEAGIPKGVFNVLPGYGHTvGNAL 231
Cdd:cd07099 158 TPLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAAL 192
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
40-236 |
2.40e-33 |
|
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: 125.11 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 40 ISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLN- 118
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 119 -IDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSP 197
Cdd:cd07101 79 vLDVAIVARYYARRAERLLKPRRRRGAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTA 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 2585406586 198 LTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMD 236
Cdd:cd07101 159 LTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNAD 197
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
21-237 |
3.51e-33 |
|
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: 124.99 E-value: 3.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 21 RAYINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEE 100
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLT--WGQTSLAQRTSVLLRYQALLKEHRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 101 LALLETLDMGKPISDSLNiDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVT-REPVGVVGAIVPWNFPLMMACWKLG 179
Cdd:TIGR01722 80 IAELITAEHGKTHSDALG-DVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSiRQPLGVCAGITPFNFPAMIPLWMFP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2585406586 180 PALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGyGHTVGNALAVHMDV 237
Cdd:TIGR01722 159 IAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDV 215
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
23-240 |
5.70e-32 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 121.60 E-value: 5.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAvSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:PRK09457 4 WINGDWIAG-QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPA--WARLSFEERQAIVERFAALLEENKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSLN--------IDVPGAAQAlSWSGEAIDKIYDEVAATPHdqlglvtrEPVGVVGAIVPWNFPLMMA 174
Cdd:PRK09457 81 EVIARETGKPLWEAATevtaminkIAISIQAYH-ERTGEKRSEMADGAAVLRH--------RPHGVVAVFGPYNFPGHLP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2585406586 175 CWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGyGHTVGNALAVHMDVDTL 240
Cdd:PRK09457 152 NGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGL 216
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
26-234 |
2.81e-31 |
|
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: 119.72 E-value: 2.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 26 GEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLE 105
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKE--WAATLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 106 TLDMGKPISDSlNIDVpGAAQAlswsgeaidkIYDEVAATPHDQLGL------------VTREPVGVVGAIVPWNFPLMM 173
Cdd:cd07151 79 IRESGSTRIKA-NIEW-GAAMA----------ITREAATFPLRMEGRilpsdvpgkenrVYREPLGVVGVISPWNFPLHL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2585406586 174 ACWKLGPALSTGNSVILKPSEKSPLTA-IRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVH 234
Cdd:cd07151 147 SMRSVAPALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEH 208
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
58-220 |
4.49e-31 |
|
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: 118.45 E-value: 4.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 58 DAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPiSDSLNIDVPGAAQALSWSGEAIDK 137
Cdd:cd07105 1 DADQAVEAAAAAFPA--WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGAT-AAWAGFNVDLAAGMLREAASLITQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 138 IYDE-VAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGV 216
Cdd:cd07105 78 IIGGsIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGV 157
|
....
gi 2585406586 217 FNVL 220
Cdd:cd07105 158 LNVV 161
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
6-238 |
1.78e-30 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 118.76 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 6 RADWEQRAKALKiegrAYINGEYTAA----VSGDTFECISPVDGR-LLATVASCDASDAQCAVENARATFNSgvWSRLAP 80
Cdd:PRK11904 533 RSELEPLAAAIA----AFLEKQWQAGpiinGEGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPA--WSRTPV 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 81 AKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLNiDVPgaaqalswsgEAID----------KIYDEVAATP---- 146
Cdd:PRK11904 607 EERAAILERAADLLEANRAELIALCVREAGKTLQDAIA-EVR----------EAVDfcryyaaqarRLFGAPEKLPgptg 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 147 -HDQLGLVTRepvGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGH 225
Cdd:PRK11904 676 eSNELRLHGR---GVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGA 752
|
250
....*....|...
gi 2585406586 226 TVGNALAVHMDVD 238
Cdd:PRK11904 753 TVGAALTADPRIA 765
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
45-238 |
5.46e-30 |
|
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: 115.85 E-value: 5.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 45 GRLLATVASCDASDAQCAVENARATfnSGVWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLnIDVPGA 124
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAA--QRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAG-FEVGAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 125 AQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTA-IRI 203
Cdd:cd07152 78 IGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVI 157
|
170 180 190
....*....|....*....|....*....|....*
gi 2585406586 204 AALAVEAGIPKGVFNVLPGyGHTVGNALAVHMDVD 238
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVA 191
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
62-221 |
2.04e-29 |
|
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: 114.09 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 62 AVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLNiDVPGAAQALSW---SGEAIDKi 138
Cdd:cd07100 4 ALDRAHAAFLA--WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARA-EVEKCAWICRYyaeNAEAFLA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 139 yDEVAATPHDQlGLVTREPVGVVGAIVPWNFPLmmacWK----LGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPK 214
Cdd:cd07100 80 -DEPIETDAGK-AYVRYEPLGVVLGIMPWNFPF----WQvfrfAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPE 153
|
....*..
gi 2585406586 215 GVFNVLP 221
Cdd:cd07100 154 GVFQNLL 160
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
91-238 |
5.18e-29 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 112.52 E-value: 5.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 91 AALLKANAEELALLETLDMGKPISDSLnIDVPGAAQALSWSGEAIDKIYDEVaaTPHDQLG---LVTREPVGVVGAIVPW 167
Cdd:PRK10090 5 AAGIRERASEISALIVEEGGKIQQLAE-VEVAFTADYIDYMAEWARRYEGEI--IQSDRPGeniLLFKRALGVTTGILPW 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2585406586 168 NFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:PRK10090 82 NFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVA 152
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
20-237 |
5.52e-29 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 113.88 E-value: 5.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 20 GRAY---INGE--YTAavsgDTFECISPVD-GRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAAL 93
Cdd:PRK03137 34 GQDYpliIGGEriTTE----DKIVSINPANkSEVVGRVSKATKELAEKAMQAALEAFET--WKKWSPEDRARILLRAAAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 94 LKANAEELALLETLDMGKPIsdslnidvpgaAQALSWSGEAIDKI--YDEVAATPHDQLGLVTRE---------PVGVVG 162
Cdd:PRK03137 108 IRRRKHEFSAWLVKEAGKPW-----------AEADADTAEAIDFLeyYARQMLKLADGKPVESRPgehnryfyiPLGVGV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2585406586 163 AIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDV 237
Cdd:PRK03137 177 VISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKT 251
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
24-231 |
9.16e-29 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 113.88 E-value: 9.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 24 INGEytaAVSGDTFECISPVDGR-LLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:COG4230 562 IAGE---AASGEARPVRNPADHSdVVGTVVEATAADVEAALAAAQAAFPA--WSATPVEERAAILERAADLLEAHRAELM 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSLNiDVPgaaqalswsgEAID--KIY------DEVAATPHdqlglvtrEPVGVVGAIVPWNFPL--- 171
Cdd:COG4230 637 ALLVREAGKTLPDAIA-EVR----------EAVDfcRYYaaqarrLFAAPTVL--------RGRGVFVCISPWNFPLaif 697
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2585406586 172 ---MMAcwklgpALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNAL 231
Cdd:COG4230 698 tgqVAA------ALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAAL 754
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
24-234 |
3.59e-28 |
|
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: 111.54 E-value: 3.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 24 INGEYTAavSGDTFECISPVDGR-LLATVASCDASDAQCAVENARATFnsGVWSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:TIGR01238 42 IGHSYKA--DGEAQPVTNPADRRdIVGQVFHANLAHVQAAIDSAQQAF--PTWNATPAKERAAKLDRLADLLELHMPELM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSLNiDVPGAAQALSWSGEAIDkiydevaatphDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPAL 182
Cdd:TIGR01238 118 ALCVREAGKTIHNAIA-EVREAVDFCRYYAKQVR-----------DVLGEFSVESRGVFVCISPWNFPLAIFTGQISAAL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2585406586 183 STGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVH 234
Cdd:TIGR01238 186 AAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSD 237
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
62-240 |
1.01e-27 |
|
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: 109.28 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 62 AVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLnidvpGAAQALswsgeaIDKI--- 138
Cdd:cd07095 5 AVAAARAAFPG--WAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQ-----TEVAAM------AGKIdis 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 139 ---YDEVA---ATPHDQLGLVTR-EPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAG 211
Cdd:cd07095 72 ikaYHERTgerATPMAQGRAVLRhRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAG 151
|
170 180
....*....|....*....|....*....
gi 2585406586 212 IPKGVFNVLPGyGHTVGNALAVHMDVDTL 240
Cdd:cd07095 152 LPPGVLNLVQG-GRETGEALAAHEGIDGL 179
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
31-231 |
1.01e-27 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 111.11 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 31 AVSGDTFECISPVD-GRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDM 109
Cdd:PRK11905 563 DVDGGTRPVLNPADhDDVVGTVTEASAEDVERALAAAQAAFPE--WSATPAAERAAILERAADLMEAHMPELFALAVREA 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 110 GKPISDslnidvpgaaqALSWSGEAID--KIY-DEVAATPHDQlglvTREPVGVVGAIVPWNFPLMMACWKLGPALSTGN 186
Cdd:PRK11905 641 GKTLAN-----------AIAEVREAVDflRYYaAQARRLLNGP----GHKPLGPVVCISPWNFPLAIFTGQIAAALVAGN 705
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2585406586 187 SVILKPSEKSPLtairIAALAV----EAGIPKGVFNVLPGYGHTVGNAL 231
Cdd:PRK11905 706 TVLAKPAEQTPL----IAARAVrllhEAGVPKDALQLLPGDGRTVGAAL 750
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
24-237 |
8.22e-27 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 107.91 E-value: 8.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 24 INGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNsgVWSRLAPAKRKTVMIRFAALLKANAEELAL 103
Cdd:PLN02419 118 IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFP--LWRNTPITTRQRVMLKFQELIRKNMDKLAM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 104 LETLDMGKPISDS-------LNIDVPGAAQALSWSGEAIDKIYDEVaatphDQLGLvtREPVGVVGAIVPWNFPLMMACW 176
Cdd:PLN02419 196 NITTEQGKTLKDShgdifrgLEVVEHACGMATLQMGEYLPNVSNGV-----DTYSI--REPLGVCAGICPFNFPAMIPLW 268
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2585406586 177 KLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVgNALAVHMDV 237
Cdd:PLN02419 269 MFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDI 328
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
23-238 |
6.91e-26 |
|
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: 104.60 E-value: 6.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAavSGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNsgVWsRLAPA-KRKTVMIRFAALLKANAEEL 101
Cdd:cd07130 2 VYDGEWGG--GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFK--EW-RDVPApKRGEIVRQIGDALRKKKEAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 102 ALLETLDMGKPISDSLN-----IDVPGAAQALSWSgeaidkIYDEVAAT--PHDQLgLVTREPVGVVGAIVPWNFPLMMA 174
Cdd:cd07130 77 GKLVSLEMGKILPEGLGevqemIDICDFAVGLSRQ------LYGLTIPSerPGHRM-MEQWNPLGVVGVITAFNFPVAVW 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2585406586 175 CWKLGPALSTGNSVILKPSEKSPLTAI---RIAALAVEA-GIPKGVFNVLPGyGHTVGNALAVHMDVD 238
Cdd:cd07130 150 GWNAAIALVCGNVVVWKPSPTTPLTAIavtKIVARVLEKnGLPGAIASLVCG-GADVGEALVKDPRVP 216
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
21-238 |
7.66e-26 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 104.84 E-value: 7.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 21 RAYINGEYTAAVSGDTFECISPVDGRLLATVASCDASDAQCAVENARATfnSGVWSRLAPAKRKTVMIRFAALLKANAEE 100
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA--QKAWAKTPLWKRAELLHKAAAILKEHKAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 101 LALLETLDMGKPISDSLnIDVPGAAQALSWSGEAIDKIY--------DEVAATPHDQLGLVTREPVGVVGAIVPWNFPLM 172
Cdd:PLN00412 95 IAECLVKEIAKPAKDAV-TEVVRSGDLISYTAEEGVRILgegkflvsDSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVN 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2585406586 173 MACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVHMDVD 238
Cdd:PLN00412 174 LAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVN 239
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
23-234 |
1.15e-25 |
|
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: 104.20 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAavSGDTFECISPVD-GRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEEL 101
Cdd:cd07083 22 VIGGEWVD--TKERMVSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKT--WKDWPQEDRARLLLKAADLLRRRRREL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 102 ALLETLDMGKPISDSLN-----IDVP--GAAQALSWSGEAIdkiydEVAATPHDQLGLVTRePVGVVGAIVPWNFPLMMA 174
Cdd:cd07083 98 IATLTYEVGKNWVEAIDdvaeaIDFIryYARAALRLRYPAV-----EVVPYPGEDNESFYV-GLGAGVVISPWNFPVAIF 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 175 CWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVH 234
Cdd:cd07083 172 TGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEH 231
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
49-231 |
2.51e-22 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 95.43 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 49 ATVASCDASdAQCAVENARatfnsgVWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDslnidvpgaaqAL 128
Cdd:PRK11809 679 ATPAEVEQA-LESAVNAAP------IWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSN-----------AI 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 129 SWSGEAID--KIYdevAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAAL 206
Cdd:PRK11809 741 AEVREAVDflRYY---AGQVRDDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRI 817
|
170 180
....*....|....*....|....*
gi 2585406586 207 AVEAGIPKGVFNVLPGYGHTVGNAL 231
Cdd:PRK11809 818 LLEAGVPAGVVQLLPGRGETVGAAL 842
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
38-215 |
4.29e-22 |
|
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: 94.02 E-value: 4.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 38 ECISPVDGRLLATVASCDASDAQCAVENARATF-NSGVWsrLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDS 116
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFlDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 117 LnIDVPGAAQALSWSGEAIDK-----IYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILK 191
Cdd:cd07148 80 K-VEVTRAIDGVELAADELGQlggreIPMGLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180
....*....|....*....|....
gi 2585406586 192 PSEKSPLTAIRIAALAVEAGIPKG 215
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEG 182
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
40-220 |
2.08e-19 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 86.33 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 40 ISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISdSLNI 119
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFRD--YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLA-SAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 120 DVPGAAQALSWSGEAIDKIYDEVAATPHD---QLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKS 196
Cdd:PRK09406 83 EALKCAKGFRYYAEHAEALLADEPADAAAvgaSRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNV 162
|
170 180
....*....|....*....|....
gi 2585406586 197 PLTAIRIAALAVEAGIPKGVFNVL 220
Cdd:PRK09406 163 PQTALYLADLFRRAGFPDGCFQTL 186
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
40-220 |
3.39e-19 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 85.68 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 40 ISPVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSlNI 119
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA-RA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 120 DVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLT 199
Cdd:PRK13968 89 EVAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGC 168
|
170 180
....*....|....*....|.
gi 2585406586 200 AIRIAALAVEAGIPKGVFNVL 220
Cdd:PRK13968 169 AQLIAQVFKDAGIPQGVYGWL 189
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
73-238 |
5.34e-17 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 79.20 E-value: 5.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 73 GVWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLNIDVPGAA----QALSWSGEAIDKIYDEVAATPHD 148
Cdd:cd07084 13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQlrarAFVIYSYRIPHEPGNHLGQGLKQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 149 QLGLVtREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGI-PKGVFNVLPGYGHTv 227
Cdd:cd07084 93 QSHGY-RWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLINGDGKT- 170
|
170
....*....|.
gi 2585406586 228 GNALAVHMDVD 238
Cdd:cd07084 171 MQALLLHPNPK 181
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
62-222 |
7.64e-17 |
|
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: 78.80 E-value: 7.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 62 AVENARATFNSGvwsRLAP-AKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLNIDVPGAAQALSWSGEAIDK-IY 139
Cdd:cd07135 10 IHSRLRATFRSG---KTKDlEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKwAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 140 DEVAATPHDQLGL----VTREPVGVVGAIVPWNFPLMMAcwkLGP---ALSTGNSVILKPSEKSPLTAIRIAALaVEAGI 212
Cdd:cd07135 87 DEKVKDGPLAFMFgkprIRKEPLGVVLIIGPWNYPVLLA---LSPlvgAIAAGCTVVLKPSELTPHTAALLAEL-VPKYL 162
|
170
....*....|
gi 2585406586 213 PKGVFNVLPG 222
Cdd:cd07135 163 DPDAFQVVQG 172
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
42-241 |
5.03e-15 |
|
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: 73.49 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 42 PVDGRLLATVASCDASDAQCAVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSLNIDV 121
Cdd:cd07098 3 PATGQHLGSVPADTPEDVDEAIAAARAAQRE--WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 122 PGAAQALSWSgeaIDkiYDEVAATPHDQLG---------LVTREPVGVVGAIVPWNFPLMMAcwkLGPALS---TGNSVI 189
Cdd:cd07098 81 LVTCEKIRWT---LK--HGEKALRPESRPGgllmfykraRVEYEPLGVVGAIVSWNYPFHNL---LGPIIAalfAGNAIV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2585406586 190 LKPSE-----KSPLTAIRIAALAvEAGIPKGVFNVLPGYGHTvGNALAVHMDVDTLV 241
Cdd:cd07098 153 VKVSEqvawsSGFFLSIIRECLA-ACGHDPDLVQLVTCLPET-AEALTSHPVIDHIT 207
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
62-222 |
5.05e-15 |
|
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: 73.33 E-value: 5.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 62 AVENARATFNSGvwsRLAPAK-RKTVMIRFAALLKANAEEL--ALLEtlDMGKPISDSLNIDVPGAAQALSwsgEAIDKI 138
Cdd:cd07087 3 LVARLRETFLTG---KTRSLEwRKAQLKALKRMLTENEEEIaaALYA--DLGKPPAEAYLTEIAVVLGEID---HALKHL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 139 YD-----EVAATPHDQLG--LVTREPVGVVGAIVPWNFPLMMAcwkLGP---ALSTGNSVILKPSEKSPLTAIRIAALaV 208
Cdd:cd07087 75 KKwmkprRVSVPLLLQPAkaYVIPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKL-I 150
|
170
....*....|....
gi 2585406586 209 EAGIPKGVFNVLPG 222
Cdd:cd07087 151 PKYFDPEAVAVVEG 164
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
11-234 |
4.46e-14 |
|
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: 70.69 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 11 QRAKALKIEGRAYINGE--YTaavsGDTFECISPVD-GRLLATVASCDASDAQCAVENARATfnSGVWSRLAPAKRKTVM 87
Cdd:cd07123 24 AELKSLTVEIPLVIGGKevRT----GNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEA--RKEWARMPFEDRAAIF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 88 IRFAALLKANAEELALLET-LDMGKPISDSlNIDVpgAAqalswsgEAID----------KIY-DEVAATPHDQLGLVTR 155
Cdd:cd07123 98 LKAADLLSGKYRYELNAATmLGQGKNVWQA-EIDA--AC-------ELIDflrfnvkyaeELYaQQPLSSPAGVWNRLEY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 156 EPV-GVVGAIVPWNFPLMMACWKLGPALsTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNALAVH 234
Cdd:cd07123 168 RPLeGFVYAVSPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLAS 246
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
153-206 |
4.56e-14 |
|
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: 70.59 E-value: 4.56e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2585406586 153 VTREPVGVVGAIVPWNFPLMMAcwkLGP---ALSTGNSVILKPSEKSPLTAIRIAAL 206
Cdd:cd07133 97 VEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSALLAEL 150
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
55-231 |
9.48e-13 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 66.98 E-value: 9.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 55 DASDAQCAVENARATFNSGVWSRLApaKRKTVMIRFAALLKANAEELALLETLDMGKP--ISDSLNIDVP-GAAQAL--- 128
Cdd:PTZ00381 5 NPEIIPPIVKKLKESFLTGKTRPLE--FRKQQLRNLLRMLEENKQEFSEAVHKDLGRHpfETKMTEVLLTvAEIEHLlkh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 129 --SWSGEaiDKIYDEVAATPHDqlGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAAL 206
Cdd:PTZ00381 83 ldEYLKP--EKVDTVGVFGPGK--SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKL 158
|
170 180
....*....|....*....|....*
gi 2585406586 207 aVEAGIPKGVFNVLPGyGHTVGNAL 231
Cdd:PTZ00381 159 -LTKYLDPSYVRVIEG-GVEVTTEL 181
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
156-217 |
9.74e-12 |
|
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: 63.78 E-value: 9.74e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2585406586 156 EPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVF 217
Cdd:cd07134 99 EPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA 160
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
62-214 |
1.86e-11 |
|
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: 63.01 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 62 AVENARATFNSGvwsRLAPAK-RKTVMIRFAALLKANAEELalLETL--DMGKPISDSLNIDVPGAAQALSwsgEAIDKI 138
Cdd:cd07132 3 AVRRAREAFSSG---KTRPLEfRIQQLEALLRMLEENEDEI--VEALakDLRKPKFEAVLSEILLVKNEIK---YAISNL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 139 yDEVAATPHDQLGLVT--------REPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALavea 210
Cdd:cd07132 75 -PEWMKPEPVKKNLATllddvyiyKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL---- 149
|
....
gi 2585406586 211 gIPK 214
Cdd:cd07132 150 -IPK 152
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
22-233 |
1.21e-10 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 60.62 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 22 AYINGEYTAavSGDTFECISPVDGRLLATVASCDASDAQcavENARATFNSG-VWSRLAPAKRKTVMIRFAALLKANAEE 100
Cdd:PLN02315 23 CYVGGEWRA--NGPLVSSVNPANNQPIAEVVEASLEDYE---EGLRACEEAAkIWMQVPAPKRGEIVRQIGDALRAKLDY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 101 LALLETLDMGKPISDSLN-----IDVPGAAQALS--WSGEAIdkiydevAATPHDQLGLVTREPVGVVGAIVPWNFPLMM 173
Cdd:PLN02315 98 LGRLVSLEMGKILAEGIGevqeiIDMCDFAVGLSrqLNGSII-------PSERPNHMMMEVWNPLGIVGVITAFNFPCAV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2585406586 174 ACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEA----GIPKGVFNVLPGyGHTVGNALAV 233
Cdd:PLN02315 171 LGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAK 233
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
63-215 |
1.58e-10 |
|
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: 60.12 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 63 VENARATFNSGvwsRLAPAK-RKTVMIRFAALLKANaeELALLETL--DMGKPISDS----LNIDVPGAAQALS----WS 131
Cdd:cd07137 5 VRELRETFRSG---RTRSAEwRKSQLKGLLRLVDEN--EDDIFAALrqDLGKPSAESfrdeVSVLVSSCKLAIKelkkWM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 132 geAIDKIYDEVAATPHDqlGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAAL----- 206
Cdd:cd07137 80 --APEKVKTPLTTFPAK--AEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLipeyl 155
|
170
....*....|....*
gi 2585406586 207 ------AVEAGIPKG 215
Cdd:cd07137 156 dtkaikVIEGGVPET 170
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
63-214 |
3.03e-09 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 56.66 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 63 VENARATFNSGVWSRLApaKRKTVMIRFAALLKANAEEL--ALLEtlDMGK----PISDSLNIDVPGAAQALSWSGE--A 134
Cdd:PLN02203 12 VAELRETYESGRTRSLE--WRKSQLKGLLRLLKDNEEAIfkALHQ--DLGKhrveAYRDEVGVLTKSANLALSNLKKwmA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 135 IDKIYDEVAATPHDqlGLVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAiriAALAveAGIPK 214
Cdd:PLN02203 88 PKKAKLPLVAFPAT--AEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATS---AFLA--ANIPK 160
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
151-231 |
6.41e-09 |
|
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: 55.59 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 151 GLVTREPVGVVGAIVPWNFPLMMAcwkLGP---ALSTGNSVILKPSEKSPLTAIRIAALaVEAGIPKGVFNVLPGyGHTV 227
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKI-IEETFDEEYVAVVEG-GVEE 168
|
....
gi 2585406586 228 GNAL 231
Cdd:cd07136 169 NQEL 172
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
62-234 |
3.25e-07 |
|
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: 50.23 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 62 AVENARATFNSgvWSRLAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISdSLNIDVP-------GAAQAL---SWS 131
Cdd:cd07129 4 AAAAAAAAFES--YRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEA-RLQGELGrttgqlrLFADLVregSWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 132 GEAIDKIYDEVAATPHDQLGLVtREPVGVVGAIVPWNFPLmmACWKLG----PALSTGNSVILKPSEKSPLTAIRIAALA 207
Cdd:cd07129 81 DARIDPADPDRQPLPRPDLRRM-LVPLGPVAVFGASNFPL--AFSVAGgdtaSALAAGCPVVVKAHPAHPGTSELVARAI 157
|
170 180 190
....*....|....*....|....*....|.
gi 2585406586 208 VEA----GIPKGVFNVLPGYGHTVGNALAVH 234
Cdd:cd07129 158 RAAlratGLPAGVFSLLQGGGREVGVALVKH 188
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
23-222 |
1.82e-06 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 48.16 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAvSGDTFECISPVDGRLLATVAScDASDAQCAVENARATFNSGVwSRLAPAKRKTVMIRFAALLKANAEELA 102
Cdd:PRK11903 8 YVAGRWQAG-SGAGTPLFDPVTGEELVRVSA-TGLDLAAAFAFAREQGGAAL-RALTYAQRAALLAAIVKVLQANRDAYY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLETLDMGKPISDSlNIDVPGAAQALSWSGEAIDKIYDEVAATPHDQLGLvTREPV-----------GVVGAIVPWNFPL 171
Cdd:PRK11903 85 DIATANSGTTRNDS-AVDIDGGIFTLGYYAKLGAALGDARLLRDGEAVQL-GKDPAfqgqhvlvptrGVALFINAFNFPA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2585406586 172 MMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGI-PKGVFNVLPG 222
Cdd:PRK11903 163 WGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCG 214
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
153-206 |
1.94e-06 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 48.12 E-value: 1.94e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2585406586 153 VTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAAL 206
Cdd:PLN02174 108 IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL 161
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
23-222 |
9.18e-06 |
|
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: 46.11 E-value: 9.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAvSGDTFECISPVDGRLLATVAScDASDAQCAVENARATfnsGvwsrlAPAKRKTVMIRFAALLKANAeeLA 102
Cdd:cd07128 4 YVAGQWHAG-TGDGRTLHDAVTGEVVARVSS-EGLDFAAAVAYAREK---G-----GPALRALTFHERAAMLKALA--KY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 103 LLE--------TLDMGKPISDSLnIDVPGAAQAL-SWSGEAIDKIYDEVAAT--PHDQLG----------LVTREPVGVv 161
Cdd:cd07128 72 LMErkedlyalSAATGATRRDSW-IDIDGGIGTLfAYASLGRRELPNAHFLVegDVEPLSkdgtfvgqhiLTPRRGVAV- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2585406586 162 gAIVPWNFPlmmaCW----KLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGI-PKGVFNVLPG 222
Cdd:cd07128 150 -HINAFNFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICG 210
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
78-241 |
1.09e-05 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 45.68 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 78 LAPAKRKTVMIRFAALLKANAEELALLETLDMGKPISDSlnidvpgAAQALSWSGEAIDKIYDEVAA------------- 144
Cdd:cd07077 13 NHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSL-------IANWIAMMGCSESKLYKNIDTergitasvghiqd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 145 -TPHDQLGLVTR-EPVGVVGAIVPWNFPLMmACWKLGPALSTGNSVILKPSEKSPLTAiRIAAL----AVEAGIPKGVFN 218
Cdd:cd07077 86 vLLPDNGETYVRaFPIGVTMHILPSTNPLS-GITSALRGIATRNQCIFRPHPSAPFTN-RALALlfqaADAAHGPKILVL 163
|
170 180
....*....|....*....|...
gi 2585406586 219 VLPGYGHTVGNALAVHMDVDTLV 241
Cdd:cd07077 164 YVPHPSDELAEELLSHPKIDLIV 186
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
23-231 |
2.44e-05 |
|
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: 44.79 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 23 YINGEYTAAvsGDTFECISPVDGRLLATVASCDASDAQCAVENARATFNSGVWSRLAPAKR----KTVMIRFAALLKANA 98
Cdd:cd07126 2 LVAGKWKGA--SNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKNPERyllyGDVSHRVAHELRKPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 99 EELALLETLDMGKPISDslnidvpgaAQALswsGEAI--DKIYDEVA-----------ATPHDQLGLV---TREPVGVVG 162
Cdd:cd07126 80 VEDFFARLIQRVAPKSD---------AQAL---GEVVvtRKFLENFAgdqvrflarsfNVPGDHQGQQssgYRWPYGPVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2585406586 163 AIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAALAVEAGIPKGVFNVLPGYGHTVGNAL 231
Cdd:cd07126 148 IITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKIL 216
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
156-241 |
1.63e-04 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 42.09 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 156 EPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAAL----AVEAGIPKGVFNVLPGYGHTVGNAL 231
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKImreaAVAAGAPEGLIQWIEEPSIELTQEL 173
|
90
....*....|
gi 2585406586 232 AVHMDVDTLV 241
Cdd:cd07122 174 MKHPDVDLIL 183
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
152-241 |
1.22e-03 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 39.56 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 152 LVTREPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPSEKSPLTAIRIAAL----AVEAGIPKGVFNVLPGYGHTV 227
Cdd:cd07081 90 LIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLllqaAVAAGAPENLIGWIDNPSIEL 169
|
90
....*....|....
gi 2585406586 228 GNALAVHMDVDTLV 241
Cdd:cd07081 170 AQRLMKFPGIGLLL 183
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
148-239 |
1.44e-03 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 39.40 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585406586 148 DQLGLVT-REPVGVVGAIVPWNFPLMMACWKLGPALSTGNSVILKPS---EKSPLTAIRIA-ALAVEAGIPKGVFNVLPG 222
Cdd:PRK13805 98 DEFGIIEiAEPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHpraQKSSIAAAKIVlDAAVAAGAPKDIIQWIEE 177
|
90
....*....|....*..
gi 2585406586 223 YGHTVGNALAVHMDVDT 239
Cdd:PRK13805 178 PSVELTNALMNHPGIAL 194
|
|
| |
