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Conserved domains on  [gi|2713496845|ref|WP_340439404|]
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aldehyde dehydrogenase family protein, partial [Pseudomonas aeruginosa]

Protein Classification

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 ...
 1-93 8.19e-72

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 cd07559:

Pssm-ID: 448367 [Multi-domain]  Cd Length: 480  Bit Score: 220.29  E-value: 8.19e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:cd07559    85 TLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 164

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:cd07559   165 NTVVLKPASQTPL 177
 
Name Accession Description Interval E-value
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
 1-93 8.19e-72

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: 220.29  E-value: 8.19e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:cd07559    85 TLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 164

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:cd07559   165 NTVVLKPASQTPL 177
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 1-93 1.33e-41

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: 141.42  E-value: 1.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLnADIPLAADHFRYFAGCIRAQEGSAAEINDS-TVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAA 79
Cdd:COG1012    90 TLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSDAPgTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAA 168

                          90
                  ....*....|....
gi 2713496845  80 GNCVVLKPAEQTPL 93
Cdd:COG1012   169 GNTVVLKPAEQTPL 182
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
 1-93 5.00e-41

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: 139.59  E-value: 5.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLnADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:pfam00171  76 TLENGKPLAEAR-GEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAG 154

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:pfam00171 155 NTVVLKPSELTPL 167
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
5-93 1.16e-37

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 130.80  E-value: 1.16e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   5 GKAVRETLNADIPLAADHFRYFAGCIRAQEGSAA-EINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCV 83
Cdd:PRK13473   90 GKPLHLALNDEIPAIVDVFRFFAGAARCLEGKAAgEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTV 169

                          90
                  ....*....|
gi 2713496845  84 VLKPAEQTPL 93
Cdd:PRK13473  170 VLKPSEITPL 179
ABALDH TIGR03374
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ...
 5-93 5.11e-33

1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1.35), also called gamma-aminobutyraldehyde dehydrogenase. This enzyme can follow putrescine transaminase (EC 2.6.1.82) for a two-step conversion of putrescine to gamma-aminobutyric acid (GABA). The member from Escherichia coli is characterized as a homotetramer that binds one NADH per momomer. This enzyme belongs to the medium-chain aldehyde dehydrogenases, and is quite similar in sequence to the betaine aldehyde dehydrogenase (EC 1.2.1.8) family.


Pssm-ID: 132417  Cd Length: 472  Bit Score: 118.56  E-value: 5.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   5 GKAVRETLNADIPLAADHFRYFAGCIRAQEGSAA-EINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCV 83
Cdd:TIGR03374  89 GKPLHSVFNDEIPAIVDVFRFFAGAARCLSGLAAgEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCV 168

                          90
                  ....*....|
gi 2713496845  84 VLKPAEQTPL 93
Cdd:TIGR03374 169 VLKPSEITPL 178
 
Name Accession Description Interval E-value
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
 1-93 8.19e-72

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: 220.29  E-value: 8.19e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:cd07559    85 TLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 164

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:cd07559   165 NTVVLKPASQTPL 177
ALDH_ACDHII-AcoD cd07116
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...
 1-93 2.27e-67

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: 208.85  E-value: 2.27e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:cd07116    85 TWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAG 164

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:cd07116   165 NCVVLKPAEQTPA 177
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
 1-93 2.16e-52

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: 169.94  E-value: 2.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:cd07117    85 TLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAG 164

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:cd07117   165 NTVVIKPSSTTSL 177
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
 1-93 1.70e-47

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: 156.99  E-value: 1.70e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:cd07091    90 SLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAG 169

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:cd07091   170 NTVVLKPAEQTPL 182
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 1-93 1.33e-41

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: 141.42  E-value: 1.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLnADIPLAADHFRYFAGCIRAQEGSAAEINDS-TVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAA 79
Cdd:COG1012    90 TLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSDAPgTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAA 168

                          90
                  ....*....|....
gi 2713496845  80 GNCVVLKPAEQTPL 93
Cdd:COG1012   169 GNTVVLKPAEQTPL 182
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
 1-93 3.07e-41

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: 140.32  E-value: 3.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:cd07142    90 TWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACG 169

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:cd07142   170 NTIVLKPAEQTPL 182
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
 1-93 5.00e-41

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: 139.59  E-value: 5.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLnADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:pfam00171  76 TLENGKPLAEAR-GEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAG 154

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:pfam00171 155 NTVVLKPSELTPL 167
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
 1-93 1.07e-39

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: 136.32  E-value: 1.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:cd07141    94 TLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACG 173

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:cd07141   174 NTVVLKPAEQTPL 186
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
 3-93 1.67e-39

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: 135.64  E-value: 1.67e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   3 DNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNC 82
Cdd:cd07115    68 DTGKPIRAARRLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNT 147

                          90
                  ....*....|.
gi 2713496845  83 VVLKPAEQTPL 93
Cdd:cd07115   148 VVLKPAELTPL 158
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
 1-93 5.53e-39

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: 134.27  E-value: 5.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:cd07112    73 TLDMGKPISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAG 152

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:cd07112   153 NSVVLKPAEQSPL 165
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
 1-93 5.79e-38

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: 131.76  E-value: 5.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:cd07144    93 ALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAG 172

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:cd07144   173 NTVVIKPAENTPL 185
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
 1-93 9.46e-38

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: 131.11  E-value: 9.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:cd07143    93 ALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAG 172

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:cd07143   173 NTIVLKPSELTPL 185
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
5-93 1.16e-37

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 130.80  E-value: 1.16e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   5 GKAVRETLNADIPLAADHFRYFAGCIRAQEGSAA-EINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCV 83
Cdd:PRK13473   90 GKPLHLALNDEIPAIVDVFRFFAGAARCLEGKAAgEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTV 169

                          90
                  ....*....|
gi 2713496845  84 VLKPAEQTPL 93
Cdd:PRK13473  170 VLKPSEITPL 179
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
 1-93 1.47e-37

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: 130.89  E-value: 1.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETlNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:cd07119    84 TLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAG 162

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:cd07119   163 NTVVIKPSEVTPL 175
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
 3-93 4.54e-37

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: 128.98  E-value: 4.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   3 DNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAA-EINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGN 81
Cdd:cd07092    68 NTGKPLHLVRDDELPGAVDNFRFFAGAARTLEGPAAgEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGN 147

                          90
                  ....*....|..
gi 2713496845  82 CVVLKPAEQTPL 93
Cdd:cd07092   148 TVVLKPSETTPL 159
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
 1-93 6.37e-37

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: 128.09  E-value: 6.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLnADIPLAADHFRYFAGCIRAQEG-SAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAA 79
Cdd:cd07078    45 TLETGKPIEEAL-GEVARAADTFRYYAGLARRLHGeVIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAA 123

                          90
                  ....*....|....
gi 2713496845  80 GNCVVLKPAEQTPL 93
Cdd:cd07078   124 GNTVVLKPSELTPL 137
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
 1-93 1.00e-34

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: 122.66  E-value: 1.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETlNADIPLAADHFRYFAGCIRAQEGSAAEIN-DSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAA 79
Cdd:cd07114    68 TRDNGKLIRET-RAQVRYLAEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAA 146

                          90
                  ....*....|....
gi 2713496845  80 GNCVVLKPAEQTPL 93
Cdd:cd07114   147 GNTVVLKPSEHTPA 160
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
 1-93 1.12e-34

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 123.76  E-value: 1.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNADIPLAADHFRYFAGCiraqegsAAEINDSTVA----YHI---HEPLGVVGQIIPWNFPLLMAAWKL 73
Cdd:PLN02466  144 TWDNGKPYEQSAKAELPMFARLFRYYAGW-------ADKIHGLTVPadgpHHVqtlHEPIGVAGQIIPWNFPLLMFAWKV 216

                          90       100
                  ....*....|....*....|
gi 2713496845  74 APALAAGNCVVLKPAEQTPL 93
Cdd:PLN02466  217 GPALACGNTIVLKTAEQTPL 236
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
 3-93 1.18e-34

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: 122.89  E-value: 1.18e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   3 DNGKAVRETLNADIPLAADHFRYFAGCIRAQEgsaaeindstVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNC 82
Cdd:cd07111   108 DNGKPIRESRDCDIPLVARHFYHHAGWAQLLD----------TELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNT 177

                          90
                  ....*....|.
gi 2713496845  83 VVLKPAEQTPL 93
Cdd:cd07111   178 VVLKPAEYTPL 188
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
 1-93 1.26e-34

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: 121.18  E-value: 1.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLnADIPLAADHFRYFAGCIRAQEGSA-AEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAA 79
Cdd:cd06534    41 TLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGPElPSPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAA 119

                          90
                  ....*....|....
gi 2713496845  80 GNCVVLKPAEQTPL 93
Cdd:cd06534   120 GNTVVLKPSELTPL 133
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
 1-93 4.04e-34

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: 121.13  E-value: 4.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:cd07093    66 SLDTGKPITLARTRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFG 145

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:cd07093   146 NTVVLKPSEWTPL 158
ABALDH TIGR03374
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ...
 5-93 5.11e-33

1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1.35), also called gamma-aminobutyraldehyde dehydrogenase. This enzyme can follow putrescine transaminase (EC 2.6.1.82) for a two-step conversion of putrescine to gamma-aminobutyric acid (GABA). The member from Escherichia coli is characterized as a homotetramer that binds one NADH per momomer. This enzyme belongs to the medium-chain aldehyde dehydrogenases, and is quite similar in sequence to the betaine aldehyde dehydrogenase (EC 1.2.1.8) family.


Pssm-ID: 132417  Cd Length: 472  Bit Score: 118.56  E-value: 5.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   5 GKAVRETLNADIPLAADHFRYFAGCIRAQEGSAA-EINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCV 83
Cdd:TIGR03374  89 GKPLHSVFNDEIPAIVDVFRFFAGAARCLSGLAAgEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCV 168

                          90
                  ....*....|
gi 2713496845  84 VLKPAEQTPL 93
Cdd:TIGR03374 169 VLKPSEITPL 178
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
 1-93 2.61e-29

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 108.43  E-value: 2.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:PRK13252   91 TLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAG 170

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:PRK13252  171 NAMIFKPSEVTPL 183
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
 1-93 3.16e-28

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 105.67  E-value: 3.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:PLN02766  107 TIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAG 186

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:PLN02766  187 CTMVVKPAEQTPL 199
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
 1-93 3.26e-28

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108 [Multi-domain]  Cd Length: 494  Bit Score: 105.36  E-value: 3.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:PRK09847  106 TLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAG 185

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:PRK09847  186 NSVILKPSEKSPL 198
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
 1-93 3.77e-28

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: 105.08  E-value: 3.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVrETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:cd07090    66 TIDNGKPI-EEARVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACG 144

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:cd07090   145 NAMVYKPSPFTPL 157
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
 3-93 1.67e-27

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: 103.08  E-value: 1.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   3 DNGKAVRETlNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNC 82
Cdd:cd07109    69 DTGKPLTQA-RADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNA 147

                          90
                  ....*....|.
gi 2713496845  83 VVLKPAEQTPL 93
Cdd:cd07109   148 VVVKPAEDAPL 158
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
 3-93 1.82e-27

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: 103.21  E-value: 1.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   3 DNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNC 82
Cdd:cd07108    68 ETGNALRTQARPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNT 147

                          90
                  ....*....|.
gi 2713496845  83 VVLKPAEQTPL 93
Cdd:cd07108   148 VVLKAAEDAPL 158
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
 3-93 4.75e-27

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: 102.04  E-value: 4.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   3 DNGKAVRETLnADIPLAADHFRYFAGC---IRAQEGSAAEINDSTVAYHI-HEPLGVVGQIIPWNFPLLMAAWKLAPALA 78
Cdd:cd07110    68 DNGKPLDEAA-WDVDDVAGCFEYYADLaeqLDAKAERAVPLPSEDFKARVrREPVGVVGLITPWNFPLLMAAWKVAPALA 146

                          90
                  ....*....|....*
gi 2713496845  79 AGNCVVLKPAEQTPL 93
Cdd:cd07110   147 AGCTVVLKPSELTSL 161
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
 5-93 1.73e-26

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: 100.40  E-value: 1.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   5 GKAVRETLnADIPLAADHFRYFAG-CIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCV 83
Cdd:cd07097    88 GKTLPEAR-GEVTRAGQIFRYYAGeALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTV 166

                          90
                  ....*....|
gi 2713496845  84 VLKPAEQTPL 93
Cdd:cd07097   167 VFKPAELTPA 176
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
 1-93 6.54e-26

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: 98.66  E-value: 6.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLnADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYH-IHEPLGVVGQIIPWNFPLLMAAWKLAPALAA 79
Cdd:cd07103    66 TLEQGKPLAEAR-GEVDYAASFLEWFAEEARRIYGRTIPSPAPGKRILvIKQPVGVVAAITPWNFPAAMITRKIAPALAA 144

                          90
                  ....*....|....
gi 2713496845  80 GNCVVLKPAEQTPL 93
Cdd:cd07103   145 GCTVVLKPAEETPL 158
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
 4-93 7.33e-26

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: 98.75  E-value: 7.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   4 NGKAVRETlNADIPLAADHFRYFAGCIRAQEgsAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCV 83
Cdd:cd07106    69 QGKPLAEA-QFEVGGAVAWLRYTASLDLPDE--VIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTV 145

                          90
                  ....*....|
gi 2713496845  84 VLKPAEQTPL 93
Cdd:cd07106   146 VLKPSPFTPL 155
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
 3-93 5.46e-24

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: 93.71  E-value: 5.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   3 DNGKAVRETLNADIPLAADHFRYFAGCIRAQEGSAAEINDS----TVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALA 78
Cdd:cd07140    94 DSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQArpnrNLTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLA 173

                          90
                  ....*....|....*
gi 2713496845  79 AGNCVVLKPAEQTPL 93
Cdd:cd07140   174 AGNTVVLKPAQVTPL 188
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
 4-93 4.59e-23

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: 91.15  E-value: 4.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   4 NGKAVRETLNADIPLAADHFRYFAGCIRAQEGS--------AAEINDSTVAyhiHEPLGVVGQIIPWNFPLLMAAWKLAP 75
Cdd:cd07089    70 VGAPVMTARAMQVDGPIGHLRYFADLADSFPWEfdlpvpalRGGPGRRVVR---REPVGVVAAITPWNFPFFLNLAKLAP 146

                          90
                  ....*....|....*...
gi 2713496845  76 ALAAGNCVVLKPAEQTPL 93
Cdd:cd07089   147 ALAAGNTVVLKPAPDTPL 164
PLN02467 PLN02467
betaine aldehyde dehydrogenase
 1-89 5.61e-23

betaine aldehyde dehydrogenase


Pssm-ID: 215260 [Multi-domain]  Cd Length: 503  Bit Score: 90.95  E-value: 5.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLnADIPLAADHFRYFAG---CIRAQEGSAAEINDSTVAYHI-HEPLGVVGQIIPWNFPLLMAAWKLAPA 76
Cdd:PLN02467   97 TLDCGKPLDEAA-WDMDDVAGCFEYYADlaeALDAKQKAPVSLPMETFKGYVlKEPLGVVGLITPWNYPLLMATWKVAPA 175

                          90
                  ....*....|...
gi 2713496845  77 LAAGNCVVLKPAE 89
Cdd:PLN02467  176 LAAGCTAVLKPSE 188
ALDH_PsfA-ACA09737 cd07120
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...
 1-93 9.07e-23

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: 90.10  E-value: 9.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETlNADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAG 80
Cdd:cd07120    67 ALENGKILGEA-RFEISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAG 145

                          90
                  ....*....|...
gi 2713496845  81 NCVVLKPAEQTPL 93
Cdd:cd07120   146 CTVVVKPAGQTAQ 158
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
 1-93 1.90e-22

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: 89.17  E-value: 1.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNADIPLAADHFRYFAGCIRA----QEGSAAEINDSTVAyhiHEPLGVVGQIIPWNFPLLMAAWKLAPA 76
Cdd:cd07139    85 TAENGMPISWSRRAQGPGPAALLRYYAALARDfpfeERRPGSGGGHVLVR---REPVGVVAAIVPWNAPLFLAALKIAPA 161

                          90
                  ....*....|....*..
gi 2713496845  77 LAAGNCVVLKPAEQTPL 93
Cdd:cd07139   162 LAAGCTVVLKPSPETPL 178
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
 3-93 2.62e-20

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: 83.19  E-value: 2.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   3 DNGKAVRETLNaDIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNC 82
Cdd:cd07107    68 DCGNPVSAMLG-DVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNT 146

                          90
                  ....*....|.
gi 2713496845  83 VVLKPAEQTPL 93
Cdd:cd07107   147 VVVKPPEQAPL 157
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
 13-93 3.61e-20

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: 82.94  E-value: 3.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845  13 NADIPLAADHFRYFAGCIRAQEgSAAEINDSTVayhIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTP 92
Cdd:cd07138    95 AAQVGLGIGHLRAAADALKDFE-FEERRGNSLV---VREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAP 170


                  .
gi 2713496845  93 L 93
Cdd:cd07138   171 L 171
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
 5-93 3.68e-20

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: 82.78  E-value: 3.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   5 GKAVRETLnADIPLAADHFRYFAGCIRAQEGS--AAEINDSTvAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNC 82
Cdd:cd07131    88 GKPLAEGR-GDVQEAIDMAQYAAGEGRRLFGEtvPSELPNKD-AMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNT 165

                          90
                  ....*....|.
gi 2713496845  83 VVLKPAEQTPL 93
Cdd:cd07131   166 VVFKPAEDTPA 176
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
 1-92 3.78e-20

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: 82.77  E-value: 3.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLnADIPLAADHFRYFAGCIRAQEG-SAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAA 79
Cdd:cd07118    68 TLESGKPISQAR-GEIEGAADLWRYAASLARTLHGdSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAA 146

                          90
                  ....*....|...
gi 2713496845  80 GNCVVLKPAEQTP 92
Cdd:cd07118   147 GCTVVVKPSEFTS 159
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
 4-93 4.22e-20

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: 82.70  E-value: 4.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   4 NGKAVRETLNaDIPLAADHFRYFAGCIRAQEGsaaEINDSTVA----YHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAA 79
Cdd:cd07088    85 QGKTLSLARV-EVEFTADYIDYMAEWARRIEG---EIIPSDRPneniFIFKVPIGVVAGILPWNFPFFLIARKLAPALVT 160

                          90
                  ....*....|....
gi 2713496845  80 GNCVVLKPAEQTPL 93
Cdd:cd07088   161 GNTIVIKPSEETPL 174
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
 1-93 7.91e-20

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: 82.01  E-value: 7.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETlNADIPLAADHFRYFAGCIRAQEGS-----AAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAP 75
Cdd:cd07145    68 TIEVGKPIKQS-RVEVERTIRLFKLAAEEAKVLRGEtipvdAYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAP 146

                          90
                  ....*....|....*...
gi 2713496845  76 ALAAGNCVVLKPAEQTPL 93
Cdd:cd07145   147 AIAVGNSVVVKPSSNTPL 164
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
 36-93 9.64e-20

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: 81.49  E-value: 9.64e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2713496845  36 SAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTPL 93
Cdd:cd07149   107 DASPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPL 164
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...
 3-93 3.66e-19

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: 79.96  E-value: 3.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   3 DNGKAvRETLNADIPLAADHFRYFAG----CIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALA 78
Cdd:cd07099    67 ETGKP-RADAGLEVLLALEAIDWAARnaprVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALA 145

                          90
                  ....*....|....*
gi 2713496845  79 AGNCVVLKPAEQTPL 93
Cdd:cd07099   146 AGNAVVLKPSEVTPL 160
ALDH_PhpJ cd07146
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...
 1-93 6.66e-19

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: 79.33  E-value: 6.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLnADIPLAADHFRYFAGCIRAQEGSAAEINDST-----VAYHIHEPLGVVGQIIPWNFPLLMAAWKLAP 75
Cdd:cd07146    65 TLESGLCLKDTR-YEVGRAADVLRFAAAEALRDDGESFSCDLTAngkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAP 143

                          90
                  ....*....|....*...
gi 2713496845  76 ALAAGNCVVLKPAEQTPL 93
Cdd:cd07146   144 AIAANNRIVLKPSEKTPL 161
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
 1-93 8.92e-19

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: 79.19  E-value: 8.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLnADIPLAADHFRYFAGCIRAQEGSAAE-INDSTVAYHiHEPLGVVGQIIPWNFPLLMAAWKLAPALAA 79
Cdd:cd07124   116 VLEVGKNWAEAD-ADVAEAIDFLEYYAREMLRLRGFPVEmVPGEDNRYV-YRPLGVGAVISPWNFPLAILAGMTTAALVT 193

                          90
                  ....*....|....
gi 2713496845  80 GNCVVLKPAEQTPL 93
Cdd:cd07124   194 GNTVVLKPAEDTPV 207
putA PRK11809
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ...
 8-93 9.97e-19

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


Pssm-ID: 236989 [Multi-domain]  Cd Length: 1318  Bit Score: 78.86  E-value: 9.97e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845    8 VRE---TLN---ADIPLAADHFRYFAGCIRAQEGsaaeiNDStvayhiHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGN 81
Cdd:PRK11809   729 VREagkTFSnaiAEVREAVDFLRYYAGQVRDDFD-----NDT------HRPLGPVVCISPWNFPLAIFTGQVAAALAAGN 797

                           90
                   ....*....|..
gi 2713496845   82 CVVLKPAEQTPL 93
Cdd:PRK11809   798 SVLAKPAEQTPL 809
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
 24-93 1.30e-18

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: 78.64  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845  24 RYFAGCiraqegsAAEINDSTV-------------AYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQ 90
Cdd:cd07113   108 RYFAGW-------ATKINGETLapsipsmqgerytAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEF 180


                  ...
gi 2713496845  91 TPL 93
Cdd:cd07113   181 TPL 183
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
 49-92 2.67e-18

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: 77.57  E-value: 2.67e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2713496845  49 IHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTP 92
Cdd:cd07104    95 RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTP 138
gabD2 PRK09407
succinic semialdehyde dehydrogenase; Reviewed
 2-93 3.06e-18

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236501 [Multi-domain]  Cd Length: 524  Bit Score: 77.61  E-value: 3.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   2 WDNGK----AVRETLnaDIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPAL 77
Cdd:PRK09407  102 LETGKarrhAFEEVL--DVALTARYYARRAPKLLAPRRRAGALPVLTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPAL 179

                          90
                  ....*....|....*.
gi 2713496845  78 AAGNCVVLKPAEQTPL 93
Cdd:PRK09407  180 LAGNAVVLKPDSQTPL 195
ALDH_F3-13-14_CALDH-like cd07087
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...
 46-92 6.32e-18

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: 76.41  E-value: 6.32e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2713496845  46 AYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTP 92
Cdd:cd07087    94 AYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAP 140
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
 1-93 8.32e-18

succinic semialdehyde dehydrogenase


Pssm-ID: 215157 [Multi-domain]  Cd Length: 498  Bit Score: 76.27  E-value: 8.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNaDIPLAADHFRYFAGciraqEG--SAAEINDSTVA----YHIHEPLGVVGQIIPWNFPLLMAAWKLA 74
Cdd:PLN02278  109 TLEQGKPLKEAIG-EVAYGASFLEYFAE-----EAkrVYGDIIPSPFPdrrlLVLKQPVGVVGAITPWNFPLAMITRKVG 182

                          90
                  ....*....|....*....
gi 2713496845  75 PALAAGNCVVLKPAEQTPL 93
Cdd:PLN02278  183 PALAAGCTVVVKPSELTPL 201
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
 51-92 1.48e-17

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: 75.42  E-value: 1.48e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2713496845  51 EPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTP 92
Cdd:cd07151   129 EPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTP 170
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
 52-93 2.33e-17

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: 74.91  E-value: 2.33e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2713496845  52 PLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTPL 93
Cdd:cd07086   133 PLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPL 174
PutA2 COG4230
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
1-93 5.10e-17

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


Pssm-ID: 443374 [Multi-domain]  Cd Length: 1156  Bit Score: 74.20  E-value: 5.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845    1 TWDNGKA-VREtlnadiplAADHFRYFAGCIRAQEGSAaeindstvayHIHEPLGVVGQIIPWNFPLL-----MAAwkla 74
Cdd:COG4230    646 TLPDAIAeVRE--------AVDFCRYYAAQARRLFAAP----------TVLRGRGVFVCISPWNFPLAiftgqVAA---- 703

                           90
                   ....*....|....*....
gi 2713496845   75 pALAAGNCVVLKPAEQTPL 93
Cdd:COG4230    704 -ALAAGNTVLAKPAEQTPL 721
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
 1-93 8.87e-17

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: 73.24  E-value: 8.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLnADIPLAADHFRYFAGCIRAQEGS-----AAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAP 75
Cdd:cd07094    68 ACEGGKPIKDAR-VEVDRAIDTLRLAAEEAERIRGEeipldATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAP 146

                          90
                  ....*....|....*...
gi 2713496845  76 ALAAGNCVVLKPAEQTPL 93
Cdd:cd07094   147 AIATGCPVVLKPASKTPL 164
ALDH_EDX86601 cd07102
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...
 1-93 1.19e-16

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: 73.05  E-value: 1.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLNaDIPLAADHFRYFagcIRAQEGSAAEINDSTVA----YHIHEPLGVVGQIIPWNFPLLMAAWKLAPA 76
Cdd:cd07102    65 TWQMGRPIAQAGG-EIRGMLERARYM---ISIAEEALADIRVPEKDgferYIRREPLGVVLIIAPWNYPYLTAVNAVIPA 140

                          90
                  ....*....|....*..
gi 2713496845  77 LAAGNCVVLKPAEQTPL 93
Cdd:cd07102   141 LLAGNAVILKHSPQTPL 157
ALDH_SSADH2_GabD2 cd07101
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...
 2-93 1.22e-16

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: 73.11  E-value: 1.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   2 WDNGKAVRETLN--ADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAA 79
Cdd:cd07101    66 LETGKARRHAFEevLDVAIVARYYARRAERLLKPRRRRGAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLA 145

                          90
                  ....*....|....
gi 2713496845  80 GNCVVLKPAEQTPL 93
Cdd:cd07101   146 GNAVVLKPDSQTAL 159
PRK11905 PRK11905
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
 1-93 2.40e-16

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


Pssm-ID: 237018 [Multi-domain]  Cd Length: 1208  Bit Score: 72.20  E-value: 2.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845    1 TWDNGKA-VREtlnadiplAADHFRYFAgciraQEGSAAEINDStvayhiHEPLGVVGQIIPWNFPLLMAAWKLAPALAA 79
Cdd:PRK11905   643 TLANAIAeVRE--------AVDFLRYYA-----AQARRLLNGPG------HKPLGPVVCISPWNFPLAIFTGQIAAALVA 703

                           90
                   ....*....|....
gi 2713496845   80 GNCVVLKPAEQTPL 93
Cdd:PRK11905   704 GNTVLAKPAEQTPL 717
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
 46-93 2.90e-16

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: 71.78  E-value: 2.90e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2713496845  46 AYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTPL 93
Cdd:cd07085   130 TYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPG 177
ALDH_PutA-P5CDH cd07125
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...
 5-93 6.20e-16

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: 71.07  E-value: 6.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   5 GKAVRETLnADIPLAADHFRYFAGciRAQEGSAAEINDSTVAYH---IHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGN 81
Cdd:cd07125   120 GKTLADAD-AEVREAIDFCRYYAA--QARELFSDPELPGPTGELnglELHGRGVFVCISPWNFPLAIFTGQIAAALAAGN 196

                          90
                  ....*....|..
gi 2713496845  82 CVVLKPAEQTPL 93
Cdd:cd07125   197 TVIAKPAEQTPL 208
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
 44-92 1.08e-15

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: 70.44  E-value: 1.08e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2713496845  44 TVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTP 92
Cdd:cd07150   111 TVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETP 159
PRK10090 PRK10090
aldehyde dehydrogenase A; Provisional
 20-92 1.38e-15

aldehyde dehydrogenase A; Provisional


Pssm-ID: 182233 [Multi-domain]  Cd Length: 409  Bit Score: 69.77  E-value: 1.38e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2713496845  20 ADHFRYFAGCIRAQEGsaaEINDSTVA----YHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTP 92
Cdd:PRK10090   38 ADYIDYMAEWARRYEG---EIIQSDRPgeniLLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTP 111
ALDH_CALDH_CalB cd07133
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ...
 46-92 1.90e-15

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: 69.44  E-value: 1.90e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2713496845  46 AYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTP 92
Cdd:cd07133    95 AEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTP 141
ALDH_BenzADH cd07152
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...
 52-92 2.59e-15

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: 69.24  E-value: 2.59e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2713496845  52 PLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTP 92
Cdd:cd07152   110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTP 150
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
 5-92 5.26e-15

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: 68.26  E-value: 5.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   5 GKAVRETLnADIPLAADHFRYFAgciraqEGSAAEINDSTV------AYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALA 78
Cdd:cd07100    50 GKPIAEAR-AEVEKCAWICRYYA------ENAEAFLADEPIetdagkAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLM 122

                          90
                  ....*....|....
gi 2713496845  79 AGNCVVLKPAEQTP 92
Cdd:cd07100   123 AGNTVLLKHASNVP 136
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
 52-93 6.76e-15

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: 68.04  E-value: 6.76e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2713496845  52 PLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTPL 93
Cdd:cd07147   123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPL 164
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
 47-92 1.24e-14

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 67.36  E-value: 1.24e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2713496845  47 YHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTP 92
Cdd:PTZ00381  104 YIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSP 149
ALDH_AlkH-like cd07134
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...
 44-92 3.36e-14

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: 66.10  E-value: 3.36e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2713496845  44 TVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTP 92
Cdd:cd07134    92 TKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTP 140
ALDH_SaliADH cd07105
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...
 15-92 4.52e-14

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: 65.68  E-value: 4.52e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2713496845  15 DIPLAADHFRYFAG-CIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTP 92
Cdd:cd07105    60 NVDLAAGMLREAASlITQIIGGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSP 138
PRK03137 PRK03137
1-pyrroline-5-carboxylate dehydrogenase; Provisional
 3-93 4.63e-14

1-pyrroline-5-carboxylate dehydrogenase; Provisional


Pssm-ID: 179543  Cd Length: 514  Bit Score: 65.73  E-value: 4.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   3 DNGKAVRETlNADIPLAADHFRYFA-GCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGN 81
Cdd:PRK03137  122 EAGKPWAEA-DADTAEAIDFLEYYArQMLKLADGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGN 200

                          90
                  ....*....|..
gi 2713496845  82 CVVLKPAEQTPL 93
Cdd:PRK03137  201 TVLLKPASDTPV 212
ALDH_F14-YMR110C cd07135
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ...
 3-92 5.57e-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: 65.32  E-value: 5.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   3 DNGKAVRETLNADIPLAADHFRYFAGCIRaQEGSAAEINDSTVAYHIH------EPLGVVGQIIPWNFPLLMAAWKLAPA 76
Cdd:cd07135    54 DLGRPPFETLLTEVSGVKNDILHMLKNLK-KWAKDEKVKDGPLAFMFGkprirkEPLGVVLIIGPWNYPVLLALSPLVGA 132

                          90
                  ....*....|....*.
gi 2713496845  77 LAAGNCVVLKPAEQTP 92
Cdd:cd07135   133 IAAGCTVVLKPSELTP 148
PRK11904 PRK11904
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
1-93 2.40e-13

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


Pssm-ID: 237017 [Multi-domain]  Cd Length: 1038  Bit Score: 63.68  E-value: 2.40e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845    1 TWDNGKA-VREtlnadiplAADHFRYFAGCIRAQEGSAAEINDST-VAYHIH-EPLGVVGQIIPWNFPLLMAAWKLAPAL 77
Cdd:PRK11904   638 TLQDAIAeVRE--------AVDFCRYYAAQARRLFGAPEKLPGPTgESNELRlHGRGVFVCISPWNFPLAIFLGQVAAAL 709

                           90
                   ....*....|....*.
gi 2713496845   78 AAGNCVVLKPAEQTPL 93
Cdd:PRK11904   710 AAGNTVIAKPAEQTPL 725
ALDH_F11_NP-GAPDH cd07082
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...
 51-93 2.50e-13

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: 63.36  E-value: 2.50e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2713496845  51 EPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTPL 93
Cdd:cd07082   140 EPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVL 182
D1pyr5carbox3 TIGR01238
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ...
 5-93 4.03e-13

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: 63.01  E-value: 4.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   5 GKAVRE---TLN---ADIPLAADHFRYFAGCIRaqegsaaeindSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALA 78
Cdd:TIGR01238 118 ALCVREagkTIHnaiAEVREAVDFCRYYAKQVR-----------DVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALA 186

                          90
                  ....*....|....*
gi 2713496845  79 AGNCVVLKPAEQTPL 93
Cdd:TIGR01238 187 AGNTVIAKPAEQTSL 201
gabD PRK11241
NADP-dependent succinate-semialdehyde dehydrogenase I;
1-92 4.84e-13

NADP-dependent succinate-semialdehyde dehydrogenase I;


Pssm-ID: 183050 [Multi-domain]  Cd Length: 482  Bit Score: 62.62  E-value: 4.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETlNADIPLAADHFRYFAgciraQEGSaaEINDSTVAYH--------IHEPLGVVGQIIPWNFPLLMAAWK 72
Cdd:PRK11241   95 TLEQGKPLAEA-KGEISYAASFIEWFA-----EEGK--RIYGDTIPGHqadkrlivIKQPIGVTAAITPWNFPAAMITRK 166

                          90       100
                  ....*....|....*....|
gi 2713496845  73 LAPALAAGNCVVLKPAEQTP 92
Cdd:PRK11241  167 AGPALAAGCTMVLKPASQTP 186
ALDH_YwdH-P39616 cd07136
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ...
 46-92 5.90e-13

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: 62.52  E-value: 5.90e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2713496845  46 AYHIHEPLGVVGQIIPWNFPLLMAawkLAP---ALAAGNCVVLKPAEQTP 92
Cdd:cd07136    94 SYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTP 140
D1pyr5carbox2 TIGR01237
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ...
 5-93 6.83e-12

delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]


Pssm-ID: 200087 [Multi-domain]  Cd Length: 511  Bit Score: 59.49  E-value: 6.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   5 GKAVRETlNADIPLAADHFRYFA-GCIRAQEGSAAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCV 83
Cdd:TIGR01237 120 GKPWNEA-DAEVAEAIDFMEYYArQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCV 198

                          90
                  ....*....|
gi 2713496845  84 VLKPAEQTPL 93
Cdd:TIGR01237 199 VLKPAEAAPV 208
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
 50-92 9.28e-12

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: 59.16  E-value: 9.28e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2713496845  50 HEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTP 92
Cdd:cd07132    98 KEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSP 140
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
 52-93 1.12e-11

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: 58.76  E-value: 1.12e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2713496845  52 PLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTPL 93
Cdd:cd07130   132 PLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPL 173
ALDH_F3FHI cd07137
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ...
 49-92 4.88e-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: 57.04  E-value: 4.88e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2713496845  49 IHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTP 92
Cdd:cd07137    98 VSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAP 141
PLN02419 PLN02419
methylmalonate-semialdehyde dehydrogenase [acylating]
 1-92 2.46e-10

methylmalonate-semialdehyde dehydrogenase [acylating]


Pssm-ID: 166060 [Multi-domain]  Cd Length: 604  Bit Score: 55.14  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETlNADIPLAADHFRYFAGCIRAQEGS-AAEINDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAA 79
Cdd:PLN02419  198 TTEQGKTLKDS-HGDIFRGLEVVEHACGMATLQMGEyLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTC 276

                          90
                  ....*....|...
gi 2713496845  80 GNCVVLKPAEQTP 92
Cdd:PLN02419  277 GNTFILKPSEKDP 289
gabD1 PRK09406
succinic semialdehyde dehydrogenase; Reviewed
 1-92 3.12e-10

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181826 [Multi-domain]  Cd Length: 457  Bit Score: 54.74  E-value: 3.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETlNADIPLAADHFRYFAGciRAQEGSAAEIND-----STVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAP 75
Cdd:PRK09406   70 TLEMGKTLASA-KAEALKCAKGFRYYAE--HAEALLADEPADaaavgASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAP 146

                          90
                  ....*....|....*..
gi 2713496845  76 ALAAGNCVVLKPAEQTP 92
Cdd:PRK09406  147 ALMAGNVGLLKHASNVP 163
ALDH_F15-22 cd07098
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ...
 43-91 3.23e-10

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: 54.61  E-value: 3.23e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2713496845  43 STVAYHihePLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQT 91
Cdd:cd07098   114 ARVEYE---PLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQV 159
PLN02203 PLN02203
aldehyde dehydrogenase
 51-92 1.17e-09

aldehyde dehydrogenase


Pssm-ID: 165847 [Multi-domain]  Cd Length: 484  Bit Score: 53.19  E-value: 1.17e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2713496845  51 EPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTP 92
Cdd:PLN02203  107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAP 148
PLN00412 PLN00412
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
 52-90 1.23e-09

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 215110 [Multi-domain]  Cd Length: 496  Bit Score: 53.22  E-value: 1.23e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2713496845  52 PLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQ 90
Cdd:PLN00412  158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQ 196
MMSDH TIGR01722
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ...
 47-93 1.24e-09

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: 52.96  E-value: 1.24e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2713496845  47 YHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTPL 93
Cdd:TIGR01722 131 YSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPS 177
ALDH_P5CDH cd07083
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...
 1-93 1.24e-09

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: 52.97  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   1 TWDNGKAVRETLnADIPLAADHFRYFAGCIRAQEGSAAEINDSTVAYH--IHEPLGVVGQIIPWNFPLLMAAWKLAPALA 78
Cdd:cd07083   102 TYEVGKNWVEAI-DDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNesFYVGLGAGVVISPWNFPVAIFTGMIVAPVA 180

                          90
                  ....*....|....*
gi 2713496845  79 AGNCVVLKPAEQTPL 93
Cdd:cd07083   181 VGNTVIAKPAEDAVV 195
ALDH_RL0313 cd07148
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...
 7-93 1.99e-09

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: 52.42  E-value: 1.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   7 AVRETLNA--DIPLAADHFRYFAGCIRAQEGSAAeiNDSTVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVV 84
Cdd:cd07148    79 AKVEVTRAidGVELAADELGQLGGREIPMGLTPA--SAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVI 156


                  ....*....
gi 2713496845  85 LKPAEQTPL 93
Cdd:cd07148   157 VKPALATPL 165
ALDH_SGSD_AstD cd07095
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...
 50-93 2.61e-09

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: 52.27  E-value: 2.61e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2713496845  50 HEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTPL 93
Cdd:cd07095    95 HRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPA 138
astD PRK09457
succinylglutamic semialdehyde dehydrogenase; Reviewed
 50-92 9.51e-09

succinylglutamic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181873  Cd Length: 487  Bit Score: 50.34  E-value: 9.51e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2713496845  50 HEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTP 92
Cdd:PRK09457  132 HRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTP 174
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
 52-93 3.48e-08

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 49.06  E-value: 3.48e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2713496845  52 PLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTPL 93
Cdd:PLN02315  154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPL 195
PLN02174 PLN02174
aldehyde dehydrogenase family 3 member H1
 49-92 5.98e-08

aldehyde dehydrogenase family 3 member H1


Pssm-ID: 177831  Cd Length: 484  Bit Score: 48.50  E-value: 5.98e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2713496845  49 IHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPAEQTP 92
Cdd:PLN02174  109 VSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAP 152
ALDH_KGSADH-like cd07084
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ...
 5-93 2.97e-07

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: 46.46  E-value: 2.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2713496845   5 GKAVRETLNADIPLAADHFRYFAG-CIRAQEGSAAEIND--STVAYHIHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGN 81
Cdd:cd07084    50 GKGWMFAENICGDQVQLRARAFVIySYRIPHEPGNHLGQglKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGN 129

                          90
                  ....*....|..
gi 2713496845  82 CVVLKPAEQTPL 93
Cdd:cd07084   130 PVIVKPHTAVSI 141
PRK13968 PRK13968
putative succinate semialdehyde dehydrogenase; Provisional
 32-88 3.35e-06

putative succinate semialdehyde dehydrogenase; Provisional


Pssm-ID: 184426 [Multi-domain]  Cd Length: 462  Bit Score: 43.31  E-value: 3.35e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2713496845  32 AQEGSAAEINDSTVAYhihEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNCVVLKPA 88
Cdd:PRK13968  109 KAEPTLVENQQAVIEY---RPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHA 162
ALDH_MaoC-N cd07128
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ...
 41-91 3.75e-05

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: 40.33  E-value: 3.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2713496845  41 NDSTVAYHIHEPL-GVVGQIIPWNFPllmaAW----KLAPALAAGNCVVLKPAEQT 91
Cdd:cd07128   132 DGTFVGQHILTPRrGVAVHINAFNFP----VWgmleKFAPALLAGVPVIVKPATAT 183
 
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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