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Conserved domains on  [gi|2579478520|ref|WP_310724864|]
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aldehyde dehydrogenase family protein, partial [Burkholderia multivorans]

Protein Classification

aldehyde dehydrogenase family protein( domain architecture ID 34081)

aldehyde dehydrogenase family protein is an NAD(P)(+)-dependent enzyme that may oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and may play an important role in detoxification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ALDH-SF super family cl11961
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
 36-217 6.28e-86

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.


The actual alignment was detected with superfamily member cd07110:

Pssm-ID: 448367 [Multi-domain]  Cd Length: 456  Bit Score: 261.52  E-value: 6.28e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  36 IFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADI 115
Cdd:cd07110     1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 116 GDVAATFAYYASLCADPATFAAEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTS 195
Cdd:cd07110    81 DDVAGCFEYYADLAEQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160

                         170       180
                  ....*....|....*....|..
gi 2579478520 196 PAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07110   161 LTELELAEIAAEAGLPPGVLNV 182
 
Name Accession Description Interval E-value
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
 36-217 6.28e-86

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: 261.52  E-value: 6.28e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  36 IFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADI 115
Cdd:cd07110     1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 116 GDVAATFAYYASLCADPATFAAEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTS 195
Cdd:cd07110    81 DDVAGCFEYYADLAEQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160

                         170       180
                  ....*....|....*....|..
gi 2579478520 196 PAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07110   161 LTELELAEIAAEAGLPPGVLNV 182
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 20-217 1.94e-54

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: 180.71  E-value: 1.94e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  20 IAGRAVRTHSDtAGAPIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAAL 99
Cdd:COG1012    10 IGGEWVAAASG-ETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAAL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 100 QMQVSGKPPFEADADIGDVAATFAYYASLcadPATFAAEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPA 179
Cdd:COG1012    89 LTLETGKPLAEARGEVDRAADFLRYYAGE---ARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPA 165

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2579478520 180 LAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:COG1012   166 LAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNV 203
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
 35-217 5.11e-53

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: 176.57  E-value: 5.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  35 PIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADAD 114
Cdd:pfam00171  10 EVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 115 IGDVAATFAYYASLCAdpaTFAAEAVALPNASFAAERfHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELT 194
Cdd:pfam00171  90 VDRAIDVLRYYAGLAR---RLDGETLPSDPGRLAYTR-REPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELT 165

                         170       180
                  ....*....|....*....|...
gi 2579478520 195 SPAEHALLEIVAAAGVPAGVVNV 217
Cdd:pfam00171 166 PLTALLLAELFEEAGLPAGVLNV 188
PLN02467 PLN02467
betaine aldehyde dehydrogenase
 35-217 3.21e-50

betaine aldehyde dehydrogenase


Pssm-ID: 215260 [Multi-domain]  Cd Length: 503  Bit Score: 169.91  E-value: 3.21e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  35 PIFNASTGATIGWQEFATAMHVDDAVRAARDALAG-----WRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPF 109
Cdd:PLN02467   26 PVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 110 EADADIGDVAATFAYYASLCADPATFAAEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLK 189
Cdd:PLN02467  106 EAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLK 185

                         170       180
                  ....*....|....*....|....*...
gi 2579478520 190 PSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:PLN02467  186 PSELASVTCLELADICREVGLPPGVLNV 213
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
 29-217 1.11e-30

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: 117.22  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  29 SDTAGAP--IFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGK 106
Cdd:TIGR01804   8 EDSAGTTreIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKLETLDTGK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 107 PPFEAD-ADIGDVAATFAYYASLCadPAtFAAEAVALPNASFAAERfHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCT 185
Cdd:TIGR01804  88 TLQETIvADMDSGADVFEFFAGLA--PA-LNGEIIPLGGPSFAYTI-REPLGVCVGIGAWNYPLQIASWKIAPALAAGNA 163

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2579478520 186 VVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:TIGR01804 164 MVFKPSENTPLTALKVAEIMEEAGLPKGVFNV 195
 
Name Accession Description Interval E-value
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
 36-217 6.28e-86

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: 261.52  E-value: 6.28e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  36 IFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADI 115
Cdd:cd07110     1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 116 GDVAATFAYYASLCADPATFAAEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTS 195
Cdd:cd07110    81 DDVAGCFEYYADLAEQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160

                         170       180
                  ....*....|....*....|..
gi 2579478520 196 PAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07110   161 LTELELAEIAAEAGLPPGVLNV 182
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 20-217 1.94e-54

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: 180.71  E-value: 1.94e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  20 IAGRAVRTHSDtAGAPIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAAL 99
Cdd:COG1012    10 IGGEWVAAASG-ETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAAL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 100 QMQVSGKPPFEADADIGDVAATFAYYASLcadPATFAAEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPA 179
Cdd:COG1012    89 LTLETGKPLAEARGEVDRAADFLRYYAGE---ARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPA 165

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2579478520 180 LAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:COG1012   166 LAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNV 203
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
 35-217 5.11e-53

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: 176.57  E-value: 5.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  35 PIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADAD 114
Cdd:pfam00171  10 EVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 115 IGDVAATFAYYASLCAdpaTFAAEAVALPNASFAAERfHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELT 194
Cdd:pfam00171  90 VDRAIDVLRYYAGLAR---RLDGETLPSDPGRLAYTR-REPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELT 165

                         170       180
                  ....*....|....*....|...
gi 2579478520 195 SPAEHALLEIVAAAGVPAGVVNV 217
Cdd:pfam00171 166 PLTALLLAELFEEAGLPAGVLNV 188
PLN02467 PLN02467
betaine aldehyde dehydrogenase
 35-217 3.21e-50

betaine aldehyde dehydrogenase


Pssm-ID: 215260 [Multi-domain]  Cd Length: 503  Bit Score: 169.91  E-value: 3.21e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  35 PIFNASTGATIGWQEFATAMHVDDAVRAARDALAG-----WRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPF 109
Cdd:PLN02467   26 PVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 110 EADADIGDVAATFAYYASLCADPATFAAEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLK 189
Cdd:PLN02467  106 EAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLK 185

                         170       180
                  ....*....|....*....|....*...
gi 2579478520 190 PSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:PLN02467  186 PSELASVTCLELADICREVGLPPGVLNV 213
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
 20-217 1.84e-49

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: 167.49  E-value: 1.84e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  20 IAGRAVRTHSDTAgAPIFNASTGATIGWQEFATAMHVDDAVRAARDAL--AGWRDTPPAERGRLLAAIAERVEAERARLA 97
Cdd:cd07119     2 IDGEWVEAASGKT-RDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  98 ALQMQVSGKPPFEADADIGDVAATFAYYASLCADPAtfaAEAVALPNASFAAERfHDAVGVAALIVPWNFPMVTTAWKLA 177
Cdd:cd07119    81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKET---GEVYDVPPHVISRTV-REPVGVCGLITPWNYPLLQAAWKLA 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2579478520 178 PALAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07119   157 PALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNL 196
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
 57-217 1.10e-45

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: 156.60  E-value: 1.10e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  57 DDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIGDVAATFAYYASLCAdpaTFA 136
Cdd:cd07078     1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLAR---RLH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 137 AEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVN 216
Cdd:cd07078    78 GEVIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157


                  .
gi 2579478520 217 V 217
Cdd:cd07078   158 V 158
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
 35-217 8.43e-44

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: 152.36  E-value: 8.43e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  35 PIFNASTGATIGWQEFATAMHVDDAVRAARDAL--AGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFE-A 111
Cdd:cd07091    22 PTINPATEEVICQVAEADEEDVDAAVKAARAAFetGWWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEEsA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 112 DADIGDVAATFAYYASLcADPATfaAEAVALPNASFAAERfHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPS 191
Cdd:cd07091   102 KGDVALSIKCLRYYAGW-ADKIQ--GKTIPIDGNFLAYTR-REPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPA 177

                         170       180
                  ....*....|....*....|....*.
gi 2579478520 192 ELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07091   178 EQTPLSALYLAELIKEAGFPPGVVNI 203
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
 29-217 5.17e-43

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: 150.64  E-value: 5.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  29 SDTAGAPIFNASTGATIGWQEFATAMHVDDAVRAARDALAG-WRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKP 107
Cdd:cd07144    20 SDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 108 PFE-ADADIGDVAATFAYYASLcADPATfaAEAVALPNASFAAErFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTV 186
Cdd:cd07144   100 YHSnALGDLDEIIAVIRYYAGW-ADKIQ--GKTIPTSPNKLAYT-LHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTV 175

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2579478520 187 VLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07144   176 VIKPAENTPLSLLYFANLVKEAGFPPGVVNI 206
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
 36-217 5.95e-43

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: 150.02  E-value: 5.95e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  36 IFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADA-D 114
Cdd:cd07093     1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 115 IGDVAATFAYYASLCAdpaTFAAEAVALPNASFAAERfHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELT 194
Cdd:cd07093    81 IPRAAANFRFFADYIL---QLDGESYPQDGGALNYVL-RQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWT 156

                         170       180
                  ....*....|....*....|...
gi 2579478520 195 SPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07093   157 PLTAWLLAELANEAGLPPGVVNV 179
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
 61-217 1.77e-41

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: 144.29  E-value: 1.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  61 RAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIGDVAATFAYYASLCADPAtfaAEAV 140
Cdd:cd06534     1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLG---GPEL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2579478520 141 ALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd06534    78 PSPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNV 154
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
 36-217 2.59e-41

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: 145.39  E-value: 2.59e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  36 IFNASTGATIGWQEFATAMHVDDAVRAARDALAG--WRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADA 113
Cdd:cd07114     1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 114 DIGDVAATFAYYASLCAdpaTFAAEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSEL 193
Cdd:cd07114    81 QVRYLAEWYRYYAGLAD---KIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEH 157

                         170       180
                  ....*....|....*....|....
gi 2579478520 194 TSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07114   158 TPASTLELAKLAEEAGFPPGVVNV 181
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
 38-217 3.92e-41

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: 144.89  E-value: 3.92e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  38 NASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEA-DADIG 116
Cdd:cd07115     3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLDVP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 117 DVAATFAYYASLCAdpaTFAAEAVALpNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSP 196
Cdd:cd07115    83 RAADTFRYYAGWAD---KIEGEVIPV-RGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158

                         170       180
                  ....*....|....*....|.
gi 2579478520 197 AEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07115   159 SALRIAELMAEAGFPAGVLNV 179
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
 36-217 9.11e-41

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: 143.82  E-value: 9.11e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  36 IFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADI 115
Cdd:cd07106     1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 116 GDVAATFAYYASLCADPatfaaEAVALpNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTS 195
Cdd:cd07106    81 GGAVAWLRYTASLDLPD-----EVIED-DDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154

                         170       180
                  ....*....|....*....|..
gi 2579478520 196 PAEHALLEIVAAAgVPAGVVNV 217
Cdd:cd07106   155 LCTLKLGELAQEV-LPPGVLNV 175
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
 36-217 3.09e-40

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: 142.76  E-value: 3.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  36 IFNASTGATIGWQEFATAMHVDDAVRAARDAL-AGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADAD 114
Cdd:cd07109     1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFeSGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 115 IGDVAATFAYYASLcADpaTFAAEAVALPNASFAAERfHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELT 194
Cdd:cd07109    81 VEAAARYFEYYGGA-AD--KLHGETIPLGPGYFVYTV-REPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDA 156

                         170       180
                  ....*....|....*....|...
gi 2579478520 195 SPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07109   157 PLTALRLAELAEEAGLPAGALNV 179
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
 36-217 4.73e-40

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: 142.06  E-value: 4.73e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  36 IFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADI 115
Cdd:cd07090     1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 116 GDVAATFAYYASLCAdpaTFAAEAVALPNASFAAERfHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTS 195
Cdd:cd07090    81 DSSADCLEYYAGLAP---TLSGEHVPLPGGSFAYTR-REPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156

                         170       180
                  ....*....|....*....|..
gi 2579478520 196 PAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07090   157 LTALLLAEILTEAGLPDGVFNV 178
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
 35-217 8.23e-39

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: 139.40  E-value: 8.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  35 PIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEA-DA 113
Cdd:cd07559    19 DNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETlAA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 114 DIGDVAATFAYYASlcadpATFAAE-AVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSE 192
Cdd:cd07559    99 DIPLAIDHFRYFAG-----VIRAQEgSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPAS 173

                         170       180
                  ....*....|....*....|....*
gi 2579478520 193 LTSPAEHALLEIVAAAgVPAGVVNV 217
Cdd:cd07559   174 QTPLSILVLMELIGDL-LPKGVVNV 197
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
 35-217 1.41e-38

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: 138.63  E-value: 1.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  35 PIFNASTGATIGWQEFATAMHVDDAVRAARDAL---AGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEA 111
Cdd:cd07141    25 PTINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKS 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 112 -DADIGDVAATFAYYASlCADPATfaAEAVALPNASFAAERfHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKP 190
Cdd:cd07141   105 yLVDLPGAIKVLRYYAG-WADKIH--GKTIPMDGDFFTYTR-HEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKP 180

                         170       180
                  ....*....|....*....|....*..
gi 2579478520 191 SELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07141   181 AEQTPLTALYLASLIKEAGFPPGVVNV 207
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
 38-217 1.78e-38

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: 138.12  E-value: 1.78e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  38 NASTGATIGWQEFATAMHVDDAVRAARDALAG--WRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEA-DAD 114
Cdd:cd07112     8 NPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAlAVD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 115 IGDVAATFAYYASLC----ADPATFAAEAVALPNasfaaerfHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKP 190
Cdd:cd07112    88 VPSAANTFRWYAEAIdkvyGEVAPTGPDALALIT--------REPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159

                         170       180
                  ....*....|....*....|....*..
gi 2579478520 191 SELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07112   160 AEQSPLTALRLAELALEAGLPAGVLNV 186
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
 20-217 2.33e-38

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: 137.63  E-value: 2.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  20 IAGRAVRTHSdTAGAPIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAAL 99
Cdd:cd07138     3 IDGAWVAPAG-TETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 100 QMQVSGKPpfeadadigdvaATFAYYASLCADPATFAAEAVALPNASFAAER-----FHDAVGVAALIVPWNFPMVTTAW 174
Cdd:cd07138    82 ITLEMGAP------------ITLARAAQVGLGIGHLRAAADALKDFEFEERRgnslvVREPIGVCGLITPWNWPLNQIVL 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2579478520 175 KLAPALAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07138   150 KVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNL 192
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
 36-217 3.63e-38

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: 137.18  E-value: 3.63e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  36 IFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADI 115
Cdd:cd07103     1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 116 gDVAATFAYYaslcadpatFAAEAV-----ALPnASFAAERF---HDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVV 187
Cdd:cd07103    81 -DYAASFLEW---------FAEEARriygrTIP-SPAPGKRIlviKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVV 149

                         170       180       190
                  ....*....|....*....|....*....|
gi 2579478520 188 LKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07103   150 LKPAEETPLSALALAELAEEAGLPAGVLNV 179
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
20-217 9.23e-38

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 136.19  E-value: 9.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  20 IAGRAVRTHSDTAgaPIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAAL 99
Cdd:PRK13473    7 INGELVAGEGEKQ--PVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 100 QMQVSGKPPFEADADigDVAATfayyaslcADPATFAAEAVALPNASFAAERF--------HDAVGVAALIVPWNFPMVT 171
Cdd:PRK13473   85 ESLNCGKPLHLALND--EIPAI--------VDVFRFFAGAARCLEGKAAGEYLeghtsmirRDPVGVVASIAPWNYPLMM 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2579478520 172 TAWKLAPALAAGCTVVLKPSELTsPAEHALLEIVAAAGVPAGVVNV 217
Cdd:PRK13473  155 AAWKLAPALAAGNTVVLKPSEIT-PLTALKLAELAADILPPGVLNV 199
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
 32-216 2.76e-37

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: 135.07  E-value: 2.76e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  32 AGAPIFN-ASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFE 110
Cdd:cd07097    14 DGEENRNpSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 111 ADADIGDVAATFAYYASLCADpatFAAEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKP 190
Cdd:cd07097    94 ARGEVTRAGQIFRYYAGEALR---LSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKP 170

                         170       180
                  ....*....|....*....|....*.
gi 2579478520 191 SELTSPAEHALLEIVAAAGVPAGVVN 216
Cdd:cd07097   171 AELTPASAWALVEILEEAGLPAGVFN 196
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
 38-217 9.96e-37

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: 133.52  E-value: 9.96e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  38 NASTGATIGWQEFATAMHVDDAVRAARDALAGW-RDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIG 116
Cdd:cd07089     3 NPATEEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 117 DVAA----TFAYYASLCADPATFAAEAVALPNASFAAERfhDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSE 192
Cdd:cd07089    83 DGPIghlrYFADLADSFPWEFDLPVPALRGGPGRRVVRR--EPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160

                         170       180
                  ....*....|....*....|....*
gi 2579478520 193 LTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07089   161 DTPLSALLLGEIIAETDLPAGVVNV 185
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
 20-217 2.38e-36

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: 132.57  E-value: 2.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  20 IAGRAVRTHSDTAGApIFNASTGATIGWQEFATAMHVDDAVRAARDALAG-WRDTPPAERGRLLAAIAERVEAERARLAA 98
Cdd:cd07113     4 IDGRPVAGQSEKRLD-ITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  99 LQMQVSGKPPFEADA-DIGDVAATFAYYASLcadpAT-FAAEAVALPNASFAAER-----FHDAVGVAALIVPWNFPMVT 171
Cdd:cd07113    83 LETLCSGKSIHLSRAfEVGQSANFLRYFAGW----ATkINGETLAPSIPSMQGERytaftRREPVGVVAGIVPWNFSVMI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2579478520 172 TAWKLAPALAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07113   159 AVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNV 204
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
 27-217 6.55e-36

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: 131.42  E-value: 6.55e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  27 THSDTAGAPIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGK 106
Cdd:cd07117    11 KGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 107 PPFEA-DADIGDVAATFAYYASLCAdpaTFAAEAVALpNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCT 185
Cdd:cd07117    91 PIRETrAVDIPLAADHFRYFAGVIR---AEEGSANMI-DEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNT 166

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2579478520 186 VVLKPSELTSPAEHALLEIVAAAgVPAGVVNV 217
Cdd:cd07117   167 VVIKPSSTTSLSLLELAKIIQDV-LPKGVVNI 197
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
 20-217 5.84e-35

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: 128.85  E-value: 5.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  20 IAGRAVRThSDTAGAPIFNASTGATIGWQEFATAMHVDDAVRAARDALAG--WRDTPPAERGRLLAAIAERVEAERARLA 97
Cdd:cd07139     3 IGGRWVAP-SGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  98 ALQMQVSGKP-PFEADADIGDVAATFAYYASLCADpatFAAEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKL 176
Cdd:cd07139    82 RLWTAENGMPiSWSRRAQGPGPAALLRYYAALARD---FPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2579478520 177 APALAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07139   159 APALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNV 199
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
 35-217 6.24e-35

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: 128.67  E-value: 6.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  35 PIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEA-DA 113
Cdd:cd07111    40 PTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESrDC 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 114 DIGDVAATFAYYASLcadpATFAAEAVAlpnasfaaerFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSEL 193
Cdd:cd07111   120 DIPLVARHFYHHAGW----AQLLDTELA----------GWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEY 185

                         170       180
                  ....*....|....*....|....
gi 2579478520 194 TSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07111   186 TPLTALLFAEICAEAGLPPGVLNI 209
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
 36-217 1.02e-34

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: 127.83  E-value: 1.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  36 IFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKP-PFEADAD 114
Cdd:cd07092     1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPlHLVRDDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 115 IGDVAATFAYYASLCADPATFAAeAVALPNASFAAERfhDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELT 194
Cdd:cd07092    81 LPGAVDNFRFFAGAARTLEGPAA-GEYLPGHTSMIRR--EPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETT 157

                         170       180
                  ....*....|....*....|...
gi 2579478520 195 sPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07092   158 -PLTTLLLAELAAEVLPPGVVNV 179
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
 20-217 2.01e-34

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: 127.38  E-value: 2.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  20 IAGRAVRTHSDTAgAPIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAAL 99
Cdd:cd07088     2 INGEFVPSSSGET-IDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 100 QMQVSGKPPFEADADIGDVAATFAYYASLCAdpaTFAAEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPA 179
Cdd:cd07088    81 IVEEQGKTLSLARVEVEFTADYIDYMAEWAR---RIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPA 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2579478520 180 LAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07088   158 LVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNI 195
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
 51-217 1.41e-31

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: 119.36  E-value: 1.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  51 ATAMHVDDAVRAARDAL--AGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIGDVAATFAYYASL 128
Cdd:cd07118    16 GTVEDVDAAVAAARKAFdkGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 129 CAdpaTFAAEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSPAEHALLEIVAAA 208
Cdd:cd07118    96 AR---TLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEA 172


                  ....*....
gi 2579478520 209 GVPAGVVNV 217
Cdd:cd07118   173 GLPAGVVNI 181
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
 39-216 2.18e-31

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: 119.63  E-value: 2.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  39 ASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIGDV 118
Cdd:cd07124    54 ADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 119 AATFAYYASLcadpatfAAEAVALPNASFAAER---FHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTS 195
Cdd:cd07124   134 IDFLEYYARE-------MLRLRGFPVEMVPGEDnryVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTP 206

                         170       180
                  ....*....|....*....|.
gi 2579478520 196 PAEHALLEIVAAAGVPAGVVN 216
Cdd:cd07124   207 VIAAKLVEILEEAGLPPGVVN 227
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
 36-217 3.02e-31

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: 118.79  E-value: 3.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  36 IFNASTGATIGWQEFATAMHVDDAVRAARDALAG-W-RDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKP-PFEAD 112
Cdd:cd07143    26 VYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWgLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTfGTAKR 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 113 ADIGDVAATFAYYASLcADpaTFAAEAVALPNASFAAERfHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSE 192
Cdd:cd07143   106 VDVQASADTFRYYGGW-AD--KIHGQVIETDIKKLTYTR-HEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSE 181

                         170       180
                  ....*....|....*....|....*
gi 2579478520 193 LTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07143   182 LTPLSALYMTKLIPEAGFPPGVINV 206
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
 45-217 3.04e-31

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: 118.60  E-value: 3.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  45 IGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIGDvAATFAY 124
Cdd:cd07131    28 VGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQE-AIDMAQ 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 125 YASlcADPATFAAEAVA--LPNASfaAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSPAEHALL 202
Cdd:cd07131   107 YAA--GEGRRLFGETVPseLPNKD--AMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLV 182

                         170
                  ....*....|....*
gi 2579478520 203 EIVAAAGVPAGVVNV 217
Cdd:cd07131   183 ELFAEAGLPPGVVNV 197
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
 29-217 1.11e-30

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: 117.22  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  29 SDTAGAP--IFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGK 106
Cdd:TIGR01804   8 EDSAGTTreIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKLETLDTGK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 107 PPFEAD-ADIGDVAATFAYYASLCadPAtFAAEAVALPNASFAAERfHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCT 185
Cdd:TIGR01804  88 TLQETIvADMDSGADVFEFFAGLA--PA-LNGEIIPLGGPSFAYTI-REPLGVCVGIGAWNYPLQIASWKIAPALAAGNA 163

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2579478520 186 VVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:TIGR01804 164 MVFKPSENTPLTALKVAEIMEEAGLPKGVFNV 195
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
 35-217 1.55e-30

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: 116.82  E-value: 1.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  35 PIFNASTGATIGWQEFATAMHVDDAVRAARDAL--AGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEAD 112
Cdd:cd07142    22 PTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFdeGPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQAR 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 113 -ADIGDVAATFAYYASLCADpatfaAEAVALP-NASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKP 190
Cdd:cd07142   102 yAEVPLAARLFRYYAGWADK-----IHGMTLPaDGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKP 176

                         170       180
                  ....*....|....*....|....*..
gi 2579478520 191 SELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07142   177 AEQTPLSALLAAKLAAEAGLPDGVLNI 203
ALDH_ACDHII-AcoD cd07116
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...
 51-217 2.05e-30

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: 116.40  E-value: 2.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  51 ATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEA-DADIGDVAATFAYYASlc 129
Cdd:cd07116    35 STAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETlAADIPLAIDHFRYFAG-- 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 130 adpATFAAE-AVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSPAEHALLEIVAAA 208
Cdd:cd07116   113 ---CIRAQEgSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL 189


                  ....*....
gi 2579478520 209 gVPAGVVNV 217
Cdd:cd07116   190 -LPPGVVNV 197
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
 35-217 9.78e-30

succinic semialdehyde dehydrogenase


Pssm-ID: 215157 [Multi-domain]  Cd Length: 498  Bit Score: 114.79  E-value: 9.78e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  35 PIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEAdad 114
Cdd:PLN02278   43 PVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEA--- 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 115 IGDVAatfayYASLCADpaTFAAEAV-----ALPnASFAAERF---HDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTV 186
Cdd:PLN02278  120 IGEVA-----YGASFLE--YFAEEAKrvygdIIP-SPFPDRRLlvlKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTV 191

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2579478520 187 VLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:PLN02278  192 VVKPSELTPLTALAAAELALQAGIPPGVLNV 222
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
 20-217 2.58e-29

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: 113.38  E-value: 2.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  20 IAGRAVRTHSDTAgAPIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAAL 99
Cdd:cd07085     5 INGEWVESKTTEW-LDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 100 QMQVSGKPPFEADADIGDV--AATFAyyaslCADPATFAAEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLA 177
Cdd:cd07085    84 ITLEHGKTLADARGDVLRGleVVEFA-----CSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFP 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2579478520 178 PALAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07085   159 MAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNV 198
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
 20-217 2.36e-28

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 110.74  E-value: 2.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  20 IAGRAVrthSDTAGAPI--FNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLA 97
Cdd:PRK13252   11 IDGAYV---EATSGETFevINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  98 ALQMQVSGKPPFEAD-ADIGDVAATFAYYASLCAdpaTFAAEAVALPNASFAAERfHDAVGVAALIVPWNFPMVTTAWKL 176
Cdd:PRK13252   88 ALETLDTGKPIQETSvVDIVTGADVLEYYAGLAP---ALEGEQIPLRGGSFVYTR-REPLGVCAGIGAWNYPIQIACWKS 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2579478520 177 APALAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:PRK13252  164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNV 204
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
 36-217 5.05e-28

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: 109.76  E-value: 5.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  36 IFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEA---ERARLAALQ----MQVSGKPP 108
Cdd:cd07108     1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEArseELARLLALEtgnaLRTQARPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 109 FEADADIgdvaatFAYYASLCADpatFAAEAVALPNASFAAERfHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVL 188
Cdd:cd07108    81 AAVLADL------FRYFGGLAGE---LKGETLPFGPDVLTYTV-REPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVL 150

                         170       180
                  ....*....|....*....|....*....
gi 2579478520 189 KPSELTSPAEHALLEIVAAAgVPAGVVNV 217
Cdd:cd07108   151 KAAEDAPLAVLLLAEILAQV-LPAGVLNV 178
ALDH_PutA-P5CDH cd07125
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...
 24-217 2.37e-27

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: 108.44  E-value: 2.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  24 AVRTHSDTAGAPIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQV 103
Cdd:cd07125    39 GEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAE 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 104 SGKPPFEADADIGDvAATFAYYaslcadpatFAAEAVALPNASFAAE--------RFHdAVGVAALIVPWNFPMVTTAWK 175
Cdd:cd07125   119 AGKTLADADAEVRE-AIDFCRY---------YAAQARELFSDPELPGptgelnglELH-GRGVFVCISPWNFPLAIFTGQ 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2579478520 176 LAPALAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07125   188 IAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQL 229
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
 36-217 3.11e-27

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: 107.97  E-value: 3.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  36 IFNASTGATIGWQEFATAMHVDDAVRAARDALAG--WRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEA-D 112
Cdd:cd07140    25 TINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLAlK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 113 ADIGDVAATFAYYASLCaDPATFAAEAV--ALPNASFAAERfHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKP 190
Cdd:cd07140   105 THVGMSIQTFRYFAGWC-DKIQGKTIPInqARPNRNLTLTK-REPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKP 182

                         170       180
                  ....*....|....*....|....*..
gi 2579478520 191 SELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07140   183 AQVTPLTALKFAELTVKAGFPKGVINI 209
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
 56-217 1.32e-26

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: 105.69  E-value: 1.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  56 VDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIGDVAATFAYYASLCadpatF 135
Cdd:cd07104     2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLP-----R 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 136 AAEAVALPNASFAAER--FHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSPAEHALL-EIVAAAGVPA 212
Cdd:cd07104    77 RPEGEILPSDVPGKESmvRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEAGLPK 156


                  ....*
gi 2579478520 213 GVVNV 217
Cdd:cd07104   157 GVLNV 161
SSADH TIGR01780
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ...
 36-217 1.54e-26

succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]


Pssm-ID: 188167  Cd Length: 448  Bit Score: 105.59  E-value: 1.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  36 IFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADI 115
Cdd:TIGR01780   1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 116 GDVAATFAYYAslcADPATFAAEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTS 195
Cdd:TIGR01780  81 LYAASFLEWFA---EEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTP 157

                         170       180
                  ....*....|....*....|..
gi 2579478520 196 PAEHALLEIVAAAGVPAGVVNV 217
Cdd:TIGR01780 158 LSALALARLAEQAGIPKGVLNV 179
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...
 38-217 4.24e-26

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: 104.23  E-value: 4.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  38 NASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIGD 117
Cdd:cd07099     2 NPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 118 VAATFAYYASLCADPATFAAEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSPA 197
Cdd:cd07099    82 ALEAIDWAARNAPRVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLV 161

                         170       180
                  ....*....|....*....|
gi 2579478520 198 EHALLEIVAAAGVPAGVVNV 217
Cdd:cd07099   162 GELLAEAWAAAGPPQGVLQV 181
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
 35-217 1.56e-25

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 103.35  E-value: 1.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  35 PIFNASTGATIGWQEFATAMHVDDAVRAARDAL--AGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPpFE-- 110
Cdd:PLN02466   76 PTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFdeGPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKP-YEqs 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 111 ADADIGDVAATFAYYASLcADpatfAAEAVALP-NASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLK 189
Cdd:PLN02466  155 AKAELPMFARLFRYYAGW-AD----KIHGLTVPaDGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLK 229

                         170       180
                  ....*....|....*....|....*...
gi 2579478520 190 PSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:PLN02466  230 TAEQTPLSALYAAKLLHEAGLPPGVLNV 257
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
 9-217 1.62e-25

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 102.98  E-value: 1.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520   9 SAATFVLPAAQ-----IAGRAVrthsDTAGAPIF---NASTGATIGWQEFATAMHVDDAVRAARDAL--AGWRDTPPAER 78
Cdd:PLN02766    9 GASGVKVPEIKftklfINGEFV----DAASGKTFetrDPRTGEVIARIAEGDKEDVDLAVKAAREAFdhGPWPRMSGFER 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  79 GRLLAAIAERVEAERARLAALQMQVSGK-PPFEADADIGDVAATFAYYASlCADpaTFAAEAVALpNASFAAERFHDAVG 157
Cdd:PLN02766   85 GRIMMKFADLIEEHIEELAALDTIDAGKlFALGKAVDIPAAAGLLRYYAG-AAD--KIHGETLKM-SRQLQGYTLKEPIG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 158 VAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:PLN02766  161 VVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINV 220
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
 38-217 3.06e-25

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: 102.26  E-value: 3.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  38 NASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAErveAERARLAALQMQVS---GKPPFEAdad 114
Cdd:cd07086    19 NPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGE---ALRKKKEALGRLVSlemGKILPEG--- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 115 IGDV--AATFAYYAslcadpatfAAEAVALPNASFAAER-FHDA------VGVAALIVPWNFPMVTTAWKLAPALAAGCT 185
Cdd:cd07086    93 LGEVqeMIDICDYA---------VGLSRMLYGLTIPSERpGHRLmeqwnpLGVVGVITAFNFPVAVPGWNAAIALVCGNT 163

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2579478520 186 VVLKPSELTSPAEHALLEIVAAA----GVPAGVVNV 217
Cdd:cd07086   164 VVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNL 199
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
 37-217 4.56e-25

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: 101.64  E-value: 4.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  37 FNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADadiG 116
Cdd:cd07150     4 LNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW---F 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 117 DVAATFAYYASLCADPATFAAEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSP 196
Cdd:cd07150    81 ETTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160

                         170       180
                  ....*....|....*....|.
gi 2579478520 197 AEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07150   161 IGLKIAEIMEEAGLPKGVFNV 181
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
 34-217 4.66e-25

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: 101.66  E-value: 4.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  34 APIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADA 113
Cdd:cd07145     1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 114 DIGDVAATF---AYYASLCADpATFAAEAVALPNASFAAERFHdAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKP 190
Cdd:cd07145    81 EVERTIRLFklaAEEAKVLRG-ETIPVDAYEYNERRIAFTVRE-PIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158

                         170       180
                  ....*....|....*....|....*..
gi 2579478520 191 SELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07145   159 SSNTPLTAIELAKILEEAGLPPGVINV 185
ALDH_PsfA-ACA09737 cd07120
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...
 37-217 1.04e-24

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: 100.50  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  37 FNASTGATIGWQEFATAMHVDDAVRAARDAL--AGWRDTPpAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADAD 114
Cdd:cd07120     2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWAHDP-RLRARVLLELADAFEANAERLARLLALENGKILGEARFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 115 IGDVAATFAYYASLcadpATFAAEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELT 194
Cdd:cd07120    81 ISGAISELRYYAGL----ARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQT 156

                         170       180
                  ....*....|....*....|....
gi 2579478520 195 SPAEHALLEIVAAA-GVPAGVVNV 217
Cdd:cd07120   157 AQINAAIIRILAEIpSLPAGVVNL 180
PRK03137 PRK03137
1-pyrroline-5-carboxylate dehydrogenase; Provisional
 39-216 1.29e-24

1-pyrroline-5-carboxylate dehydrogenase; Provisional


Pssm-ID: 179543  Cd Length: 514  Bit Score: 100.78  E-value: 1.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  39 ASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIGDv 118
Cdd:PRK03137   58 ANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAE- 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 119 AATFAYYaslcadpatFAAEAVAL----PNASFAAER---FHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPS 191
Cdd:PRK03137  137 AIDFLEY---------YARQMLKLadgkPVESRPGEHnryFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPA 207

                         170       180
                  ....*....|....*....|....*
gi 2579478520 192 ELTSPAEHALLEIVAAAGVPAGVVN 216
Cdd:PRK03137  208 SDTPVIAAKFVEVLEEAGLPAGVVN 232
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
 35-217 6.27e-24

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: 98.47  E-value: 6.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  35 PIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADAD 114
Cdd:cd07147     2 EVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 115 IGDVAATFayyaslcadpaTFAAEAV------ALPNASFAA--------ERFhdAVGVAALIVPWNFPMVTTAWKLAPAL 180
Cdd:cd07147    82 VARAIDTF-----------RIAAEEAtriygeVLPLDISARgegrqglvRRF--PIGPVSAITPFNFPLNLVAHKVAPAI 148

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2579478520 181 AAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07147   149 AAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSV 185
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
 35-217 2.10e-23

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: 96.99  E-value: 2.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  35 PIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSG----KPPFE 110
Cdd:cd07151    13 DVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGstriKANIE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 111 ADADIG--DVAATFayyaslcadpaTFAAEAVALPNASFAAER--FHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTV 186
Cdd:cd07151    93 WGAAMAitREAATF-----------PLRMEGRILPSDVPGKENrvYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAV 161

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2579478520 187 VLKPSELTsPAEHALL--EIVAAAGVPAGVVNV 217
Cdd:cd07151   162 VLKPASDT-PITGGLLlaKIFEEAGLPKGVLNV 193
ALDH_SGSD_AstD cd07095
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...
 55-217 2.11e-23

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: 96.57  E-value: 2.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  55 HVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEA----DADIGDVAATFAYYASLCA 130
Cdd:cd07095     1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAqtevAAMAGKIDISIKAYHERTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 131 DPATfaaeavalPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSPAEHALLEIVAAAGV 210
Cdd:cd07095    81 ERAT--------PMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGL 152


                  ....*..
gi 2579478520 211 PAGVVNV 217
Cdd:cd07095   153 PPGVLNL 159
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
 35-217 2.46e-23

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: 96.51  E-value: 2.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  35 PIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADAD 114
Cdd:cd07149     2 EVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 115 IGDVAATFayyaSLCADPA-TFAAEAVALPNASFAAERF----HDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLK 189
Cdd:cd07149    82 VDRAIETL----RLSAEEAkRLAGETIPFDASPGGEGRIgftiREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLK 157

                         170       180
                  ....*....|....*....|....*...
gi 2579478520 190 PSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07149   158 PASQTPLSALKLAELLLEAGLPKGALNV 185
astD PRK09457
succinylglutamic semialdehyde dehydrogenase; Reviewed
 37-216 2.75e-23

succinylglutamic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181873  Cd Length: 487  Bit Score: 96.57  E-value: 2.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  37 FNASTGATIgWQ-EFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEA---- 111
Cdd:PRK09457   20 RNPVSGEVL-WQgNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAatev 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 112 DADIGDVAATFAYYASLCADPATFAAEAVALPNasfaaerfHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPS 191
Cdd:PRK09457   99 TAMINKIAISIQAYHERTGEKRSEMADGAAVLR--------HRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPS 170

                         170       180
                  ....*....|....*....|....*
gi 2579478520 192 ELTSPAEHALLEIVAAAGVPAGVVN 216
Cdd:PRK09457  171 ELTPWVAELTVKLWQQAGLPAGVLN 195
ALDH_SaliADH cd07105
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...
 55-217 2.94e-23

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: 96.11  E-value: 2.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  55 HVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIGDVAATFAYYASLCADPAT 134
Cdd:cd07105     1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 135 faaEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELtSPAEHALL-EIVAAAGVPAG 213
Cdd:cd07105    81 ---GSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASEL-SPRTHWLIgRVFHEAGLPKG 156


                  ....
gi 2579478520 214 VVNV 217
Cdd:cd07105   157 VLNV 160
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
 36-217 8.80e-23

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: 95.13  E-value: 8.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  36 IFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADI 115
Cdd:cd07107     1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 116 GDVAATFAYYASLCADpatFAAEAVALPNASFAAERfHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSElTS 195
Cdd:cd07107    81 MVAAALLDYFAGLVTE---LKGETIPVGGRNLHYTL-REPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPE-QA 155

                         170       180
                  ....*....|....*....|..
gi 2579478520 196 PAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07107   156 PLSALRLAELAREVLPPGVFNI 177
gabD2 PRK09407
succinic semialdehyde dehydrogenase; Reviewed
 1-217 1.68e-22

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236501 [Multi-domain]  Cd Length: 524  Bit Score: 94.56  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520   1 MSTVERSPSAATFVLpAAQIAGRAVRTHSDTAgaPIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGR 80
Cdd:PRK09407    4 TALPMPAPSALTFER-LRRLTARVDGAAGPTR--EVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  81 LLAAIAERVEAERARLAALQMQVSGKPPFEADADIGDVAATFAYYASLCadPATFAAEAV--ALPNASFAAERFHdAVGV 158
Cdd:PRK09407   81 VLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRA--PKLLAPRRRagALPVLTKTTELRQ-PKGV 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2579478520 159 AALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:PRK09407  158 VGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQV 216
ALDH_EDX86601 cd07102
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...
 38-217 6.00e-22

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: 92.69  E-value: 6.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  38 NASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLA---ALQMqvsGKPPFEADAD 114
Cdd:cd07102     2 SPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAeelTWQM---GRPIAQAGGE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 115 IGDVAATFAYYASLcADPATfaAEAVALPNASFaaERF--HDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSE 192
Cdd:cd07102    79 IRGMLERARYMISI-AEEAL--ADIRVPEKDGF--ERYirREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSP 153

                         170       180
                  ....*....|....*....|....*
gi 2579478520 193 LTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07102   154 QTPLCGERFAAAFAEAGLPEGVFQV 178
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
 38-217 1.35e-21

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: 91.73  E-value: 1.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  38 NASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIGD 117
Cdd:cd07094     5 NPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 118 VAATFAYYAslcADPATFAAEAVALPNASFAAERF----HDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSEL 193
Cdd:cd07094    85 AIDTLRLAA---EEAERIRGEEIPLDATQGSDNRLawtiREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161

                         170       180
                  ....*....|....*....|....
gi 2579478520 194 TSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07094   162 TPLSALELAKILVEAGVPEGVLQV 185
MMSDH TIGR01722
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ...
 20-217 6.78e-21

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: 89.94  E-value: 6.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  20 IAGRAVRTHSDTAGaPIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAAL 99
Cdd:TIGR01722   5 IGGKFAEGASGTYI-PVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 100 QMQVSGKPpfEADADiGDVAATFAYYASLCADPATFAAEAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPA 179
Cdd:TIGR01722  84 ITAEHGKT--HSDAL-GDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2579478520 180 LAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNV 198
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
 38-217 1.01e-20

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108 [Multi-domain]  Cd Length: 494  Bit Score: 89.57  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  38 NASTGATIGWQEFATAMHVDDAVRAARDAL--AGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEA-DAD 114
Cdd:PRK09847   41 DPVTQAPLAKIARGKSVDIDRAVSAARGVFerGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlRDD 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 115 IGDVAATFAYYASlcADPATFAAEAVALPNASFAAERfhDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELT 194
Cdd:PRK09847  121 IPGAARAIRWYAE--AIDKVYGEVATTSSHELAMIVR--EPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKS 196

                         170       180
                  ....*....|....*....|...
gi 2579478520 195 SPAEHALLEIVAAAGVPAGVVNV 217
Cdd:PRK09847  197 PLSAIRLAGLAKEAGLPDGVLNV 219
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
 56-214 1.40e-20

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: 88.67  E-value: 1.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  56 VDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIGDVAATFAYYaslcAD--PA 133
Cdd:cd07100     1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYY----AEnaEA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 134 TFAAEAVALPNASfaAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAG 213
Cdd:cd07100    77 FLADEPIETDAGK--AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEG 154


                  .
gi 2579478520 214 V 214
Cdd:cd07100   155 V 155
putA PRK11809
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ...
 28-215 1.07e-19

trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 236989 [Multi-domain]  Cd Length: 1318  Bit Score: 86.95  E-value: 1.07e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520   28 HSDTAGAPIFN-ASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGK 106
Cdd:PRK11809   655 VAAGEMSPVINpADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGK 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  107 PPFEADADIGDVAATFAYYASLCADpaTFAAEAvalpnasfaaerfHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTV 186
Cdd:PRK11809   735 TFSNAIAEVREAVDFLRYYAGQVRD--DFDNDT-------------HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSV 799

                          170       180
                   ....*....|....*....|....*....
gi 2579478520  187 VLKPSELTSPAEHALLEIVAAAGVPAGVV 215
Cdd:PRK11809   800 LAKPAEQTPLIAAQAVRILLEAGVPAGVV 828
PutA2 COG4230
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
17-215 2.02e-19

Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 443374 [Multi-domain]  Cd Length: 1156  Bit Score: 86.15  E-value: 2.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520   17 AAQIAGRAvrthSDTAGAPIFN-ASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERAR 95
Cdd:COG4230    559 APLIAGEA----ASGEARPVRNpADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAE 634

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520   96 LAALQMQVSGKPpfEADAdIGDV--AATFAYYaslcadpatFAAEAVALpnasFAAERFHDAVGVAALIVPWNFPMVTTA 173
Cdd:COG4230    635 LMALLVREAGKT--LPDA-IAEVreAVDFCRY---------YAAQARRL----FAAPTVLRGRGVFVCISPWNFPLAIFT 698

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2579478520  174 WKLAPALAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVV 215
Cdd:COG4230    699 GQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVL 740
gabD PRK11241
NADP-dependent succinate-semialdehyde dehydrogenase I;
35-217 2.10e-19

NADP-dependent succinate-semialdehyde dehydrogenase I;


Pssm-ID: 183050 [Multi-domain]  Cd Length: 482  Bit Score: 85.73  E-value: 2.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  35 PIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADAD 114
Cdd:PRK11241   29 DVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 115 IGdVAATFAYYaslcadpatFAAEAVALPNASFAAER-------FHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVV 187
Cdd:PRK11241  109 IS-YAASFIEW---------FAEEGKRIYGDTIPGHQadkrlivIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMV 178

                         170       180       190
                  ....*....|....*....|....*....|
gi 2579478520 188 LKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:PRK11241  179 LKPASQTPFSALALAELAIRAGIPAGVFNV 208
ALDH_SSADH2_GabD2 cd07101
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...
 41-217 2.12e-19

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: 85.44  E-value: 2.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  41 TGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIGDVAA 120
Cdd:cd07101     5 TGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 121 TFAYYASLCADPATFAAEAVALPNASFAAErFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSPAEHA 200
Cdd:cd07101    85 VARYYARRAERLLKPRRRRGAIPVLTRTTV-NRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALW 163

                         170
                  ....*....|....*..
gi 2579478520 201 LLEIVAAAGVPAGVVNV 217
Cdd:cd07101   164 AVELLIEAGLPRDLWQV 180
PRK11904 PRK11904
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
32-215 2.94e-19

bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;


Pssm-ID: 237017 [Multi-domain]  Cd Length: 1038  Bit Score: 85.64  E-value: 2.94e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520   32 AGAPIFN-ASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPpfE 110
Cdd:PRK11904   562 EARPVVSpADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKT--L 639

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  111 ADAdIGDV--AATFA-YYAS----LCADPatfaaeaVALPnaSFAAER---FHDAVGVAALIVPWNFPMVTTAWKLAPAL 180
Cdd:PRK11904   640 QDA-IAEVreAVDFCrYYAAqarrLFGAP-------EKLP--GPTGESnelRLHGRGVFVCISPWNFPLAIFLGQVAAAL 709

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2579478520  181 AAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVV 215
Cdd:PRK11904   710 AAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVL 744
PRK11905 PRK11905
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
 27-215 3.57e-19

bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 237018 [Multi-domain]  Cd Length: 1208  Bit Score: 85.30  E-value: 3.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520   27 THSDTAGAPIFN-ASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSG 105
Cdd:PRK11905   562 GDVDGGTRPVLNpADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAG 641

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  106 KPpfEADAdIGDV--AATFAYYaslcadpatFAAEAVALPNASfaaerFHDAVGVAALIVPWNFPMVTTAWKLAPALAAG 183
Cdd:PRK11905   642 KT--LANA-IAEVreAVDFLRY---------YAAQARRLLNGP-----GHKPLGPVVCISPWNFPLAIFTGQIAAALVAG 704

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2579478520  184 CTVVLKPSELTSPAEHALLEIVAAAGVPAGVV 215
Cdd:PRK11905   705 NTVLAKPAEQTPLIAARAVRLLHEAGVPKDAL 736
ALDH_P5CDH cd07083
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...
 41-216 9.11e-19

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: 83.78  E-value: 9.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  41 TGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIGDVAA 120
Cdd:cd07083    42 PSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAID 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 121 TFAYYASLCADPATFAAEAVALPNASfaAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSPAEHA 200
Cdd:cd07083   122 FIRYYARAALRLRYPAVEVVPYPGED--NESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYK 199

                         170
                  ....*....|....*.
gi 2579478520 201 LLEIVAAAGVPAGVVN 216
Cdd:cd07083   200 VFEIFHEAGFPPGVVQ 215
D1pyr5carbox3 TIGR01238
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ...
 45-215 1.24e-18

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: 83.42  E-value: 1.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  45 IGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIGDVAATFAY 124
Cdd:TIGR01238  65 VGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRY 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 125 YASLCADpatfaaeavALPNASfaaerfHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSPAEHALLEI 204
Cdd:TIGR01238 145 YAKQVRD---------VLGEFS------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVEL 209

                         170
                  ....*....|.
gi 2579478520 205 VAAAGVPAGVV 215
Cdd:TIGR01238 210 MQEAGFPAGTI 220
ALDH_F11_NP-GAPDH cd07082
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...
 35-217 4.28e-18

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: 81.85  E-value: 4.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  35 PIFNASTGATIGWQEFATAMHVDDAVRAARDALAGW-RDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPpfEADA 113
Cdd:cd07082    19 EVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWwPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKT--LKDA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 114 dIGDVAATFAY--YAslcadpatfAAEAVALPNASFAAERFHDA-----------VGVAALIVPWNFPMVTTAWKLAPAL 180
Cdd:cd07082    97 -LKEVDRTIDYirDT---------IEELKRLDGDSLPGDWFPGTkgkiaqvrrepLGVVLAIGPFNYPLNLTVSKLIPAL 166

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2579478520 181 AAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07082   167 IMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNV 203
ALDH_BenzADH cd07152
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...
 42-217 3.26e-17

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: 79.26  E-value: 3.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  42 GATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIGDVAAT 121
Cdd:cd07152     1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 122 FAYYASLCADPatfaaEAVALPNA----SFAAERfhdAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSPA 197
Cdd:cd07152    81 LHEAAGLPTQP-----QGEILPSApgrlSLARRV---PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVS 152

                         170       180
                  ....*....|....*....|.
gi 2579478520 198 EHALL-EIVAAAGVPAGVVNV 217
Cdd:cd07152   153 GGVVIaRLFEEAGLPAGVLHV 173
PRK10090 PRK10090
aldehyde dehydrogenase A; Provisional
 152-217 5.84e-16

aldehyde dehydrogenase A; Provisional


Pssm-ID: 182233 [Multi-domain]  Cd Length: 409  Bit Score: 75.54  E-value: 5.84e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2579478520 152 FHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:PRK10090   68 FKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNL 133
PLN02419 PLN02419
methylmalonate-semialdehyde dehydrogenase [acylating]
 20-217 7.26e-15

methylmalonate-semialdehyde dehydrogenase [acylating]


Pssm-ID: 166060 [Multi-domain]  Cd Length: 604  Bit Score: 72.86  E-value: 7.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  20 IAGRAVRTHSdTAGAPIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVeaeRARLAAL 99
Cdd:PLN02419  118 IGGSFVESQS-SSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELI---RKNMDKL 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 100 QMQVSGKPPFEADADIGDVAATFAYYASLCADPATFAAEAvaLPNASFAAERF--HDAVGVAALIVPWNFPMVTTAWKLA 177
Cdd:PLN02419  194 AMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEY--LPNVSNGVDTYsiREPLGVCAGICPFNFPAMIPLWMFP 271

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2579478520 178 PALAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:PLN02419  272 VAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNI 311
gabD1 PRK09406
succinic semialdehyde dehydrogenase; Reviewed
 38-214 9.85e-15

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181826 [Multi-domain]  Cd Length: 457  Bit Score: 72.08  E-value: 9.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  38 NASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIGD 117
Cdd:PRK09406    7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 118 VAATFAYYASlcaDPATFAAEAVALPNASFAAERF--HDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTS 195
Cdd:PRK09406   87 CAKGFRYYAE---HAEALLADEPADAAAVGASRAYvrYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVP 163

                         170
                  ....*....|....*....
gi 2579478520 196 PAEHALLEIVAAAGVPAGV 214
Cdd:PRK09406  164 QTALYLADLFRRAGFPDGC 182
PRK13968 PRK13968
putative succinate semialdehyde dehydrogenase; Provisional
 27-214 1.51e-14

putative succinate semialdehyde dehydrogenase; Provisional


Pssm-ID: 184426 [Multi-domain]  Cd Length: 462  Bit Score: 71.43  E-value: 1.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  27 THSDTAGAPIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGK 106
Cdd:PRK13968    2 TITPATHAISVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 107 PPFEADADIGDVAATFAYYASlcADPATFAAEAVALPNASFAAErfHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTV 186
Cdd:PRK13968   82 PINQARAEVAKSANLCDWYAE--HGPAMLKAEPTLVENQQAVIE--YRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGY 157

                         170       180
                  ....*....|....*....|....*...
gi 2579478520 187 VLKPSELTSPAEHALLEIVAAAGVPAGV 214
Cdd:PRK13968  158 LLKHAPNVMGCAQLIAQVFKDAGIPQGV 185
ALDH_PhpJ cd07146
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...
 36-217 7.86e-14

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: 69.31  E-value: 7.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  36 IFNASTGATIGWQEFATAmhvDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADI 115
Cdd:cd07146     3 VRNPYTGEVVGTVPAGTE---EALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 116 GDVAATFAYYAslcADPATFAAEAVALPNASFAAER----FHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPS 191
Cdd:cd07146    80 GRAADVLRFAA---AEALRDDGESFSCDLTANGKARkiftLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156

                         170       180
                  ....*....|....*....|....*.
gi 2579478520 192 ELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:cd07146   157 EKTPLSAIYLADLLYEAGLPPDMLSV 182
ALDH_F14-YMR110C cd07135
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ...
 105-205 8.08e-14

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: 69.56  E-value: 8.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 105 GKPPFEAD-ADIGDVAATFAYyasLCADPATFAA-EAVALPNASFAAERF---HDAVGVAALIVPWNFPMVTTAWKLAPA 179
Cdd:cd07135    56 GRPPFETLlTEVSGVKNDILH---MLKNLKKWAKdEKVKDGPLAFMFGKPrirKEPLGVVLIIGPWNYPVLLALSPLVGA 132

                          90       100
                  ....*....|....*....|....*.
gi 2579478520 180 LAAGCTVVLKPSELTSPAEHALLEIV 205
Cdd:cd07135   133 IAAGCTVVLKPSELTPHTAALLAELV 158
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
 22-217 3.93e-12

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: 64.54  E-value: 3.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  22 GRAVRTHSDTAGAPIFNASTgatigwqefATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAErveAERARLAALQM 101
Cdd:cd07130    11 GGVVTSISPANGEPIARVRQ---------ATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGD---ALRKKKEALGK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 102 QVS---GKPPFEADA------DIGDvaatFAYYASLCADPATFAAEAvalPNaSFAAERFHdAVGVAALIVPWNFPMVTT 172
Cdd:cd07130    79 LVSlemGKILPEGLGevqemiDICD----FAVGLSRQLYGLTIPSER---PG-HRMMEQWN-PLGVVGVITAFNFPVAVW 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2579478520 173 AWKLAPALAAGCTVVLKPSE---LTSPAEHALL-EIVAAAGVPAGVVNV 217
Cdd:cd07130   150 GWNAAIALVCGNVVVWKPSPttpLTAIAVTKIVaRVLEKNGLPGAIASL 198
ALDH_KGSADH-like cd07084
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ...
 59-217 5.57e-12

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: 64.18  E-value: 5.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  59 AVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEAdADIGDVAATFAYYASLCADPATFAAE 138
Cdd:cd07084     4 ALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARAFVIYSYRIPHEP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 139 AVAL-PNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTS-PAEHALLEIVAAAGVPAGVVN 216
Cdd:cd07084    83 GNHLgQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSiVMQIMVRLLHYAGLLPPEDVT 162


                  .
gi 2579478520 217 V 217
Cdd:cd07084   163 L 163
ALDH_F3FHI cd07137
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ...
 60-202 3.80e-11

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: 61.66  E-value: 3.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  60 VRAARDALAGWRDTPPAERGRLLAAIAERV-EAERARLAALQmQVSGKPPFEAdadigdvaatFAYYASLCADPATFA-- 136
Cdd:cd07137     5 VRELRETFRSGRTRSAEWRKSQLKGLLRLVdENEDDIFAALR-QDLGKPSAES----------FRDEVSVLVSSCKLAik 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2579478520 137 -------AEAVALPNASF--AAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELtSPAEHALL 202
Cdd:cd07137    74 elkkwmaPEKVKTPLTTFpaKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSEL-APATSALL 147
ALDH_F4-17_P5CDH cd07123
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ...
 9-216 4.98e-11

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: 61.45  E-value: 4.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520   9 SAATFVLPAaQIAGRAVRTHSDTAGAPIFNASTgaTIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAER 88
Cdd:cd07123    27 KSLTVEIPL-VIGGKEVRTGNTGKQVMPHDHAH--VLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  89 VEAE-RARLAALQMQVSGKPPFEADAD-IGDVAATFAYYASlcadpatFAAEAVAL-PNASFAA----------ERFhda 155
Cdd:cd07123   104 LSGKyRYELNAATMLGQGKNVWQAEIDaACELIDFLRFNVK-------YAEELYAQqPLSSPAGvwnrleyrplEGF--- 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2579478520 156 vgVAAlIVPWNFPMVTTAWKLAPALAaGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVN 216
Cdd:cd07123   174 --VYA-VSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVIN 230
ALDH_F3-13-14_CALDH-like cd07087
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...
 80-203 1.37e-10

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: 59.85  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  80 RLLAAIAERveaERARLAALQMQVsGKPPFEAD-ADIGDVAATFAYYASLCADPAtfAAEAVALPNASFAAERF--HDAV 156
Cdd:cd07087    28 ALKRMLTEN---EEEIAAALYADL-GKPPAEAYlTEIAVVLGEIDHALKHLKKWM--KPRRVSVPLLLQPAKAYviPEPL 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2579478520 157 GVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTsPAEHALLE 203
Cdd:cd07087   102 GVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELA-PATSALLA 147
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
 136-197 4.01e-10

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 58.50  E-value: 4.01e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2579478520 136 AAEAVALPNASFAAERF--HDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELtSPA 197
Cdd:PTZ00381   88 KPEKVDTVGVFGPGKSYiiPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSEL-SPH 150
ALDH_MaoC-N cd07128
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ...
 30-213 7.08e-10

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: 58.05  E-value: 7.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  30 DTAGAPIFNASTGATIGwqeFATAMHVD--DAVRAARD-ALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGK 106
Cdd:cd07128    13 TGDGRTLHDAVTGEVVA---RVSSEGLDfaAAVAYAREkGGPALRALTFHERAAMLKALAKYLMERKEDLYALSAATGAT 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 107 ppfEADA--DIGDVAATFAYYASLCA---DPATFAAEAVALP---NASFAAErfHDAV---GVAALIVPWNFPMVTTAWK 175
Cdd:cd07128    90 ---RRDSwiDIDGGIGTLFAYASLGRrelPNAHFLVEGDVEPlskDGTFVGQ--HILTprrGVAVHINAFNFPVWGMLEK 164

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2579478520 176 LAPALAAGCTVVLKPSELTSPAEHALLEIVAAAGV-PAG 213
Cdd:cd07128   165 FAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEG 203
ALDH_KGSADH cd07129
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ...
 56-216 9.15e-10

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: 57.55  E-value: 9.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  56 VDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIGDVAATFAYYASLCADPATF 135
Cdd:cd07129     1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREGSWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 136 AA-------EAVALPNASFaaERFHDAVGVAALIVPWNFPMV--TTAWKLAPALAAGCTVVLKP-------SELTSpaeH 199
Cdd:cd07129    81 DAridpadpDRQPLPRPDL--RRMLVPLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKAhpahpgtSELVA---R 155

                         170
                  ....*....|....*..
gi 2579478520 200 ALLEIVAAAGVPAGVVN 216
Cdd:cd07129   156 AIRAALRATGLPAGVFS 172
ALDH_AlkH-like cd07134
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...
 153-208 9.37e-10

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: 57.62  E-value: 9.37e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2579478520 153 HDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTsPAEHALL-EIVAAA 208
Cdd:cd07134    98 YEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELT-PHTSAVIaKIIREA 153
ALDH_F15-22 cd07098
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ...
 37-217 3.23e-09

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: 55.77  E-value: 3.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  37 FNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFeaDADIG 116
Cdd:cd07098     1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMV--DASLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 117 DVAATFAYYASLCAD-PATFAAEAVALPNASF--AAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSEL 193
Cdd:cd07098    79 EILVTCEKIRWTLKHgEKALRPESRPGGLLMFykRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQ 158

                         170       180
                  ....*....|....*....|....*...
gi 2579478520 194 TSPAEHALLEIV----AAAGVPAGVVNV 217
Cdd:cd07098   159 VAWSSGFFLSIIreclAACGHDPDLVQL 186
PLN00412 PLN00412
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
 26-217 6.19e-09

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 215110 [Multi-domain]  Cd Length: 496  Bit Score: 55.15  E-value: 6.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  26 RTHSDTAGAPIFNASTGATIGWQEFATAMHVDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSG 105
Cdd:PLN00412   25 RTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 106 KPPFEADADIGDVAATFAYYASlcaDPATFAAEAVALPNASF-AAER------FHDAVGVAALIVPWNFPMVTTAWKLAP 178
Cdd:PLN00412  105 KPAKDAVTEVVRSGDLISYTAE---EGVRILGEGKFLVSDSFpGNERnkycltSKIPLGVVLAIPPFNYPVNLAVSKIAP 181

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2579478520 179 ALAAGCTVVLKPSELTSPAEHALLEIVAAAGVPAGVVNV 217
Cdd:PLN00412  182 ALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISC 220
PLN02203 PLN02203
aldehyde dehydrogenase
 56-212 8.53e-09

aldehyde dehydrogenase


Pssm-ID: 165847 [Multi-domain]  Cd Length: 484  Bit Score: 54.73  E-value: 8.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  56 VDDAVRAARDALAGWRDTPPAERGRLLAAIAERV-EAERARLAALQmQVSGKPPFEADADIGDVAATFAYYASLCADPAT 134
Cdd:PLN02203    8 LEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLkDNEEAIFKALH-QDLGKHRVEAYRDEVGVLTKSANLALSNLKKWM 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 135 fAAEAVALPNASF--AAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELtSPAEHALLeivaAAGVPA 212
Cdd:PLN02203   87 -APKKAKLPLVAFpaTAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSEL-APATSAFL----AANIPK 160
PRK11903 PRK11903
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
76-217 9.49e-09

3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;


Pssm-ID: 237016 [Multi-domain]  Cd Length: 521  Bit Score: 54.71  E-value: 9.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  76 AERGRLLAAIAERVEAERARLAALQMQVSGKPPFEADADIGDVAATFAYYASLCAD----PATFAAEAVAL-PNASFAAE 150
Cdd:PRK11903   63 AQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAAlgdaRLLRDGEAVQLgKDPAFQGQ 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2579478520 151 RFH-DAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSPAEHALLEIVAAAGV-PAGVVNV 217
Cdd:PRK11903  143 HVLvPTRGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSV 211
ALDH_CALDH_CalB cd07133
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ...
 157-208 1.11e-08

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: 54.41  E-value: 1.11e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2579478520 157 GVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTsPAEHALL-EIVAAA 208
Cdd:cd07133   103 GVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFT-PRTSALLaELLAEY 154
ALDH_YwdH-P39616 cd07136
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ...
 157-208 1.37e-07

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: 50.97  E-value: 1.37e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2579478520 157 GVAALIVPWNFPMVTTawkLAP---ALAAGCTVVLKPSELTSPAEHALLEIVAAA 208
Cdd:cd07136   102 GVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET 153
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
 58-205 9.87e-07

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: 48.37  E-value: 9.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  58 DAVRAARDALAGWRdTPPAE-RGRLLAAIAERV-EAERARLAALQMQVsGKPPFEA-----DADIGDVAATFAYYASLCA 130
Cdd:cd07132     2 EAVRRAREAFSSGK-TRPLEfRIQQLEALLRMLeENEDEIVEALAKDL-RKPKFEAvlseiLLVKNEIKYAISNLPEWMK 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2579478520 131 DpatfaaEAVA--LPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELTSPAEHALLEIV 205
Cdd:cd07132    80 P------EPVKknLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELI 150
ALDH_RL0313 cd07148
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...
 38-213 2.84e-05

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: 44.33  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  38 NASTGATIGWQEFATAMHVDDAVRAARdALAGWRDT--PPAERGRLLAAIAERVEAERARLAALQMQVSGKP----PFEA 111
Cdd:cd07148     5 NPFDLKPIGEVPTVDWAAIDKALDTAH-ALFLDRNNwlPAHERIAILERLADLMEERADELALLIAREGGKPlvdaKVEV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 112 DADIGDVaatfayyaSLCADP-ATFAAEAVALPNASFAAER----FHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTV 186
Cdd:cd07148    84 TRAIDGV--------ELAADElGQLGGREIPMGLTPASAGRiaftTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPV 155

                         170       180
                  ....*....|....*....|....*..
gi 2579478520 187 VLKPSELTSPAEHALLEIVAAAGVPAG 213
Cdd:cd07148   156 IVKPALATPLSCLAFVDLLHEAGLPEG 182
PLN02174 PLN02174
aldehyde dehydrogenase family 3 member H1
 148-202 1.18e-04

aldehyde dehydrogenase family 3 member H1


Pssm-ID: 177831  Cd Length: 484  Bit Score: 42.34  E-value: 1.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2579478520 148 AAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKPSELtSPAEHALL 202
Cdd:PLN02174  105 SAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSEL-APASSALL 158
ALDH_F20_ACDH_EutE-like cd07081
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ...
 56-215 5.90e-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: 37.25  E-value: 5.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520  56 VDDAVRAARDALAGWRDTPPAERGRLLAAIAERVEAERARLAALQMQVSGKPPFEaDADIGDVAATFAYYASLCADPATf 135
Cdd:cd07081     1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVE-DKVIKNHFAAEYIYNVYKDEKTC- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579478520 136 aaeAVALPNASFAAERFHDAVGVAALIVPWNFPMVTTAWKLAPALAAGCTVVLKP----SELTSPAEHALLEIVAAAGVP 211
Cdd:cd07081    79 ---GVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAP 155


                  ....
gi 2579478520 212 AGVV 215
Cdd:cd07081   156 ENLI 159
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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