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Conserved domains on  [gi|2747583660|ref|WP_350669766|]
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aldehyde dehydrogenase family protein, partial [Pseudoalteromonas sp. 43-MNA-CIBAN-0464]

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 ...
 1-75 6.53e-47

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 PRK09457:

Pssm-ID: 448367  Cd Length: 487  Bit Score: 154.73  E-value: 6.53e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2747583660   1 GHILHEQFAGQPGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKGDEILARLI 75
Cdd:PRK09457  225 GYLLHRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDAFLARLV 299
 
Name Accession Description Interval E-value
astD PRK09457
succinylglutamic semialdehyde dehydrogenase; Reviewed
 1-75 6.53e-47

succinylglutamic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181873  Cd Length: 487  Bit Score: 154.73  E-value: 6.53e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2747583660   1 GHILHEQFAGQPGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKGDEILARLI 75
Cdd:PRK09457  225 GYLLHRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDAFLARLV 299
arg_catab_astD TIGR03240
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are ...
 1-75 1.21e-43

succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are succinylglutamic semialdehyde dehydrogenase (EC 1.2.1.71), the fourth enzyme in the arginine succinyltransferase (AST) pathway for arginine catabolism. [Energy metabolism, Amino acids and amines]


Pssm-ID: 274486  Cd Length: 484  Bit Score: 146.01  E-value: 1.21e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2747583660   1 GHILHEQFAGQPGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKGDEILARLI 75
Cdd:TIGR03240 223 GTLLHRQFGGRPEKILALEMGGNNPLIVDEVADIDAAVHHIIQSAFISAGQRCTCARRLLVPDGAQGDAFLARLV 297
ALDH_SGSD_AstD cd07095
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...
 1-75 1.31e-41

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: 139.71  E-value: 1.31e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2747583660   1 GHILHEQFAGQPGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKGDEILARLI 75
Cdd:cd07095   188 GLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDGAVGDAFLERLV 262
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
 1-75 2.37e-16

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: 71.41  E-value: 2.37e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2747583660   1 GHILHEQfAGQPGKILALEMGGNNPLIV-KDAEDTLAvVHDIVQSAFISSGQRCTCARKLFLPTGAKgDEILARLI 75
Cdd:pfam00171 218 GRHIAEA-AAQNLKRVTLELGGKNPLIVlEDADLDAA-VEAAVFGAFGNAGQVCTATSRLLVHESIY-DEFVEKLV 290
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 1-75 5.05e-15

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: 67.46  E-value: 5.05e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2747583660   1 GHILHEQfAGQPGKILALEMGGNNPLIV-KDAeDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKgDEILARLI 75
Cdd:COG1012   233 GRRIAAA-AAENLKRVTLELGGKNPAIVlDDA-DLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIY-DEFVERLV 305
 
Name Accession Description Interval E-value
astD PRK09457
succinylglutamic semialdehyde dehydrogenase; Reviewed
 1-75 6.53e-47

succinylglutamic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181873  Cd Length: 487  Bit Score: 154.73  E-value: 6.53e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2747583660   1 GHILHEQFAGQPGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKGDEILARLI 75
Cdd:PRK09457  225 GYLLHRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDAFLARLV 299
arg_catab_astD TIGR03240
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are ...
 1-75 1.21e-43

succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are succinylglutamic semialdehyde dehydrogenase (EC 1.2.1.71), the fourth enzyme in the arginine succinyltransferase (AST) pathway for arginine catabolism. [Energy metabolism, Amino acids and amines]


Pssm-ID: 274486  Cd Length: 484  Bit Score: 146.01  E-value: 1.21e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2747583660   1 GHILHEQFAGQPGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKGDEILARLI 75
Cdd:TIGR03240 223 GTLLHRQFGGRPEKILALEMGGNNPLIVDEVADIDAAVHHIIQSAFISAGQRCTCARRLLVPDGAQGDAFLARLV 297
ALDH_SGSD_AstD cd07095
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...
 1-75 1.31e-41

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: 139.71  E-value: 1.31e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2747583660   1 GHILHEQFAGQPGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKGDEILARLI 75
Cdd:cd07095   188 GLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDGAVGDAFLERLV 262
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
 1-75 2.37e-16

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: 71.41  E-value: 2.37e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2747583660   1 GHILHEQfAGQPGKILALEMGGNNPLIV-KDAEDTLAvVHDIVQSAFISSGQRCTCARKLFLPTGAKgDEILARLI 75
Cdd:pfam00171 218 GRHIAEA-AAQNLKRVTLELGGKNPLIVlEDADLDAA-VEAAVFGAFGNAGQVCTATSRLLVHESIY-DEFVEKLV 290
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 1-75 5.05e-15

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: 67.46  E-value: 5.05e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2747583660   1 GHILHEQfAGQPGKILALEMGGNNPLIV-KDAeDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKgDEILARLI 75
Cdd:COG1012   233 GRRIAAA-AAENLKRVTLELGGKNPAIVlDDA-DLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIY-DEFVERLV 305
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
 1-74 1.40e-14

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: 66.08  E-value: 1.40e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2747583660   1 GHILHEQfAGQPGKILALEMGGNNPLIV-KDAeDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKgDEILARL 74
Cdd:cd07078   188 GKAIMRA-AAENLKRVTLELGGKSPLIVfDDA-DLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIY-DEFVERL 259
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
 1-76 2.39e-13

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: 62.63  E-value: 2.39e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2747583660   1 GHILHEQfAGQPGKILALEMGGNNPLIV-KDAeDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKgDEILARLIT 76
Cdd:cd06534   184 GKAIMKA-AAENLKPVTLELGGKSPVIVdEDA-DLDAAVEGAVFGAFFNAGQICTAASRLLVHESIY-DEFVEKLVT 257
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
 1-74 3.88e-13

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: 62.20  E-value: 3.88e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2747583660   1 GHILHEQFAGQPGKILaLEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKgDEILARL 74
Cdd:cd07086   228 GRRVGETVARRFGRVL-LELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVY-DEFLERL 299
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
 7-75 2.43e-12

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: 60.05  E-value: 2.43e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2747583660   7 QFAGQPGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKgDEILARLI 75
Cdd:cd07131   232 ETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVY-DEFLKRFV 299
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
 1-75 2.06e-11

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: 57.26  E-value: 2.06e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2747583660   1 GHILHEQfAGQPGKILALEMGGNNPLIV-KDAEDTLAVVHdIVQSAFISSGQRCTCARKLFLPTGAKgDEILARLI 75
Cdd:cd07097   227 GRRIAAA-AAARGARVQLEMGGKNPLVVlDDADLDLAVEC-AVQGAFFSTGQRCTASSRLIVTEGIH-DRFVEALV 299
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
 1-76 7.21e-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: 55.68  E-value: 7.21e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2747583660   1 GHILHEQFAGQPGKILaLEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKgDEILARLIT 76
Cdd:cd07130   227 GRQVGQAVAARFGRSL-LELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIY-DEVLERLKK 300
PRK11904 PRK11904
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
2-76 8.62e-11

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


Pssm-ID: 237017 [Multi-domain]  Cd Length: 1038  Bit Score: 55.59  E-value: 8.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747583660    2 HILHEQFAGQPGKILAL--EMGGNNPLIVkdaeDTLA----VVHDIVQSAFISSGQRCTCARKLFLPtgakgDEILARLI 75
Cdd:PRK11904   777 RIINRTLAARDGPIVPLiaETGGQNAMIV----DSTAlpeqVVDDVVTSAFRSAGQRCSALRVLFVQ-----EDIADRVI 847


                   .
gi 2747583660   76 T 76
Cdd:PRK11904   848 E 848
ALDH_P5CDH cd07083
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...
 16-75 8.71e-10

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: 52.58  E-value: 8.71e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747583660  16 LALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAkGDEILARLI 75
Cdd:cd07083   266 LYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGA-YEPVLERLL 324
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
 1-57 1.41e-09

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: 52.22  E-value: 1.41e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2747583660   1 GHILHEQFA-GQPG----KILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCT-CAR 57
Cdd:cd07124   258 GLRIYERAAkVQPGqkwlKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSaCSR 320
PutA2 COG4230
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
2-76 3.74e-09

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


Pssm-ID: 443374 [Multi-domain]  Cd Length: 1156  Bit Score: 51.09  E-value: 3.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747583660    2 HILHEQFAGQPGKILAL--EMGGNNPLIVkdaeDTLA----VVHDIVQSAFISSGQRCTCARKLFLPtgakgDEILARLI 75
Cdd:COG4230    773 RLINRTLAARDGPIVPLiaETGGQNAMIV----DSSAlpeqVVDDVLASAFDSAGQRCSALRVLCVQ-----EDIADRVL 843


                   .
gi 2747583660   76 T 76
Cdd:COG4230    844 E 844
ALDH_PutA-P5CDH cd07125
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...
 9-61 4.18e-09

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: 50.66  E-value: 4.18e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2747583660   9 AGQPGKILAL--EMGGNNPLIVkdaeDTLA----VVHDIVQSAFISSGQRCTCARKLFL 61
Cdd:cd07125   267 AERDGPILPLiaETGGKNAMIV----DSTAlpeqAVKDVVQSAFGSAGQRCSALRLLYL 321
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
 14-62 1.76e-08

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: 49.06  E-value: 1.76e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2747583660  14 KILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLP 62
Cdd:cd07106   216 KRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVH 264
ALDH_PhpJ cd07146
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...
 1-60 4.31e-08

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: 47.74  E-value: 4.31e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747583660   1 GHILHEQfAGqpGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLF 60
Cdd:cd07146   212 GKAIAAT-AG--YKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRIL 268
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
 9-64 7.03e-08

succinic semialdehyde dehydrogenase


Pssm-ID: 215157 [Multi-domain]  Cd Length: 498  Bit Score: 47.38  E-value: 7.03e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2747583660   9 AGQPGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTG 64
Cdd:PLN02278  259 AAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEG 314
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
 14-74 1.15e-07

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: 46.55  E-value: 1.15e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2747583660  14 KILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGaKGDEILARL 74
Cdd:cd07092   221 KRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHES-VYDEFVAAL 280
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
 9-60 1.46e-07

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: 46.57  E-value: 1.46e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2747583660   9 AGQPGKILALEMGGNNPLIV-KDAeDTLAVVHDIVQSAFISSGQRCTCARKLF 60
Cdd:cd07145   222 AGGTGKKVALELGGSDPMIVlKDA-DLERAVSIAVRGRFENAGQVCNAVKRIL 273
gabD PRK11241
NADP-dependent succinate-semialdehyde dehydrogenase I;
1-64 2.05e-07

NADP-dependent succinate-semialdehyde dehydrogenase I;


Pssm-ID: 183050 [Multi-domain]  Cd Length: 482  Bit Score: 46.05  E-value: 2.05e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2747583660   1 GHILHEQFAGQPGKIlALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTG 64
Cdd:PRK11241  238 GRQLMEQCAKDIKKV-SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDG 300
putA PRK11809
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ...
 9-61 2.27e-07

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


Pssm-ID: 236989 [Multi-domain]  Cd Length: 1318  Bit Score: 45.73  E-value: 2.27e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2747583660    9 AGQPGKILAlEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFL 61
Cdd:PRK11809   874 QGRPIPLIA-ETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCL 925
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
 9-59 2.72e-07

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: 45.78  E-value: 2.72e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2747583660   9 AGQPGKILALEMGGNNPLIV-KDAEDTLAVvhDI-VQSAFISSGQRCTCARKL 59
Cdd:cd07150   218 AGRHLKKITLELGGKNPLIVlADADLDYAV--RAaAFGAFMHQGQICMSASRI 268
ALDH_SSADH2_GabD2 cd07101
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...
 17-73 2.96e-07

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: 45.38  E-value: 2.96e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2747583660  17 ALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPtGAKGDEILAR 73
Cdd:cd07101   223 SLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVH-ESVYDEFVRR 278
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
 12-60 3.05e-07

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: 45.50  E-value: 3.05e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2747583660  12 PGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLF 60
Cdd:cd07094   223 GGKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIY 271
PRK03137 PRK03137
1-pyrroline-5-carboxylate dehydrogenase; Provisional
 11-57 3.91e-07

1-pyrroline-5-carboxylate dehydrogenase; Provisional


Pssm-ID: 179543  Cd Length: 514  Bit Score: 45.31  E-value: 3.91e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2747583660  11 QPGKI----LALEMGGNNPLIV-KDAeDTLAVVHDIVQSAFISSGQRCT-CAR 57
Cdd:PRK03137  274 QPGQIwlkrVIAEMGGKDAIVVdEDA-DLDLAAESIVASAFGFSGQKCSaCSR 325
ALDH_PsfA-ACA09737 cd07120
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...
 14-74 4.35e-07

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: 45.03  E-value: 4.35e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2747583660  14 KILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKlFLPTGAKGDEILARL 74
Cdd:cd07120   222 KRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSR-VLVQRSIADEVRDRL 281
D1pyr5carbox3 TIGR01238
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ...
 12-61 4.45e-07

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: 44.90  E-value: 4.45e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2747583660  12 PGKILAlEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFL 61
Cdd:TIGR01238 266 PVPLIA-ETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCV 314
PRK11905 PRK11905
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
 19-61 1.50e-06

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


Pssm-ID: 237018 [Multi-domain]  Cd Length: 1208  Bit Score: 43.70  E-value: 1.50e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2747583660   19 EMGGNNPLIVkdaeDTLA----VVHDIVQSAFISSGQRCTCARKLFL 61
Cdd:PRK11905   788 ETGGQNAMIV----DSSAlpeqVVADVIASAFDSAGQRCSALRVLCL 830
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
 14-60 1.52e-06

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: 43.41  E-value: 1.52e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2747583660  14 KILALEMGGNNPLIV-KDAEDTLAVvHDIVQSAFISSGQRCTCARKLF 60
Cdd:cd07088   237 TKVSLELGGKAPAIVmKDADLDLAV-KAIVDSRIINCGQVCTCAERVY 283
ALDH_RL0313 cd07148
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...
 12-74 1.55e-06

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: 43.56  E-value: 1.55e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2747583660  12 PGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTgAKGDEILARL 74
Cdd:cd07148   224 PGTRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPA-EIADDFAQRL 285
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
 14-74 1.66e-06

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: 43.32  E-value: 1.66e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2747583660  14 KILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKgDEILARL 74
Cdd:cd07093   221 KPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIY-DEFLERF 280
PRK10090 PRK10090
aldehyde dehydrogenase A; Provisional
 18-74 1.72e-06

aldehyde dehydrogenase A; Provisional


Pssm-ID: 182233 [Multi-domain]  Cd Length: 409  Bit Score: 43.19  E-value: 1.72e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2747583660  18 LEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKgDEILARL 74
Cdd:PRK10090  179 LELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIY-DQFVNRL 234
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
 9-59 1.87e-06

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: 43.29  E-value: 1.87e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2747583660   9 AGQPGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKL 59
Cdd:cd07104   198 AGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRI 248
ALDH_F11_NP-GAPDH cd07082
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...
 12-75 2.52e-06

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: 42.94  E-value: 2.52e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2747583660  12 PGKILALEMGGNNPLIV-KDAEDTLAVVHdIVQSAFISSGQRCTcARKLFLPTGAKGDEILARLI 75
Cdd:cd07082   241 PMKRLVLELGGKDPAIVlPDADLELAAKE-IVKGALSYSGQRCT-AIKRVLVHESVADELVELLK 303
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
 1-61 2.53e-06

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 42.90  E-value: 2.53e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2747583660   1 GHILHEQFAGQPGKILaLEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFL 61
Cdd:PLN02315  249 GLMVQQTVNARFGKCL-LELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLL 308
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
 14-74 2.92e-06

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: 42.58  E-value: 2.92e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2747583660  14 KILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKgDEILARL 74
Cdd:cd07149   225 KKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIY-DEFLERF 284
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
 7-53 3.34e-06

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: 42.68  E-value: 3.34e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2747583660   7 QFAGQPGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRC 53
Cdd:cd07151   228 ELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQIC 274
gabD2 PRK09407
succinic semialdehyde dehydrogenase; Reviewed
 18-74 3.44e-06

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236501 [Multi-domain]  Cd Length: 524  Bit Score: 42.56  E-value: 3.44e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2747583660  18 LEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPtGAKGDEILARL 74
Cdd:PRK09407  260 LELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVH-ESIYDEFVRAF 315
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
 9-76 2.32e-05

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: 40.05  E-value: 2.32e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2747583660   9 AGQPGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSA-FISSGQRCTCARKLFLPTgAKGDEILARLIT 76
Cdd:cd07107   214 AAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHE-SIYDEVLARVVE 281
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
 18-74 2.87e-05

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: 40.12  E-value: 2.87e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2747583660  18 LEMGGNNPLIV-KDAeDTLAVVHDIVQSAFISSGQRCTCARKLFLPTgAKGDEILARL 74
Cdd:cd07113   249 LELGGKNAAAFlKDA-DIDWVVEGLLTAGFLHQGQVCAAPERFYVHR-SKFDELVTKL 304
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
 9-75 3.02e-05

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: 39.75  E-value: 3.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2747583660   9 AGQPGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCArKLFLPTGAKGDEILARLI 75
Cdd:cd07100   194 AGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAA-KRFIVHEDVYDEFLEKFV 259
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
 1-60 3.48e-05

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: 39.72  E-value: 3.48e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2747583660   1 GHILHEQfAGQPGKILALEMGGNNPLIV-KDAeDTLAVVHDIVQSAFISSGQRCTCARKLF 60
Cdd:cd07103   209 GKLLMAQ-AADTVKRVSLELGGNAPFIVfDDA-DLDKAVDGAIASKFRNAGQTCVCANRIY 267
ALDH_F15-22 cd07098
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ...
 1-53 3.93e-05

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: 39.59  E-value: 3.93e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2747583660   1 GHILHEQFAGQPG---KILA----------LEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRC 53
Cdd:cd07098   201 PVIDHITFIGSPPvgkKVMAaaaesltpvvLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNC 266
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
 1-62 4.03e-05

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 39.63  E-value: 4.03e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2747583660   1 GHILheqFAGQP--GKILA-----------LEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLP 62
Cdd:PTZ00381  187 DHIF---FTGSPrvGKLVMqaaaenltpctLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVH 258
ALDH_SaliADH cd07105
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...
 13-60 9.88e-05

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: 38.33  E-value: 9.88e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747583660  13 GKILA-----------LEMGGNNPLIV-KDAEDTLAVVHdIVQSAFISSGQRCTCARKLF 60
Cdd:cd07105   193 GRIIAetaakhlkpvlLELGGKAPAIVlEDADLDAAANA-ALFGAFLNSGQICMSTERII 251
ALDH_BenzADH cd07152
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...
 9-53 1.09e-04

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: 38.43  E-value: 1.09e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2747583660   9 AGQPGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRC 53
Cdd:cd07152   209 AGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQIC 253
ALDH_EDX86601 cd07102
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...
 6-56 1.24e-04

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: 38.00  E-value: 1.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2747583660   6 EQFAGQPGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCtCA 56
Cdd:cd07102   211 QRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSC-CS 260
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
 18-75 3.26e-04

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: 36.90  E-value: 3.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747583660  18 LEMGGNNPLIV-KDAEDTLAVvhDIVQSA-FISSGQRCTCARKLFLPTGAKgDEILARLI 75
Cdd:cd07090   223 LELGGKSPLIIfDDADLENAV--NGAMMAnFLSQGQVCSNGTRVFVQRSIK-DEFTERLV 279
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
 18-76 3.99e-04

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 36.78  E-value: 3.99e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2747583660  18 LEMGGNNPLIV-KDAEDTLAVvhDIVQSA-FISSGQRCTCARKLFLPTGAKgDEILARLIT 76
Cdd:PRK13252  249 MELGGKSPLIVfDDADLDRAA--DIAMLAnFYSSGQVCTNGTRVFVQKSIK-AAFEARLLE 306
PLN00412 PLN00412
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
 16-75 4.22e-04

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 215110 [Multi-domain]  Cd Length: 496  Bit Score: 36.66  E-value: 4.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2747583660  16 LALEMGGNNPLIV-KDAEDTLAVVHdIVQSAFISSGQRCTcARKLFLPTGAKGDEILARLI 75
Cdd:PLN00412  261 LQMELGGKDACIVlEDADLDLAAAN-IIKGGFSYSGQRCT-AVKVVLVMESVADALVEKVN 319
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
 1-75 5.67e-04

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: 36.34  E-value: 5.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2747583660   1 GHILHEQfAGQPGK-ILALeMGGNNPLIV-KDAeDTLAVVHDIVQSAFISSGQRCTcARKLFLPTGAKGDEILARLI 75
Cdd:cd07085   227 GEYIYER-AAANGKrVQAL-GGAKNHAVVmPDA-DLEQTANALVGAAFGAAGQRCM-ALSVAVAVGDEADEWIPKLV 299
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
 9-74 9.35e-04

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: 35.68  E-value: 9.35e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2747583660   9 AGQPGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKgDEILARL 74
Cdd:cd07089   222 AAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRY-DEVVEAL 286
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
 14-75 1.11e-03

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: 35.36  E-value: 1.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2747583660  14 KILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKgDEILARLI 75
Cdd:cd07119   238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIH-DKFVAALA 298
ALDH_PAD-PaaZ cd07127
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ...
 6-62 1.69e-03

Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.


Pssm-ID: 143445  Cd Length: 549  Bit Score: 34.76  E-value: 1.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2747583660   6 EQFAGQpgKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLP 62
Cdd:cd07127   294 EANARQ--AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVP 348
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
 7-76 1.94e-03

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: 34.63  E-value: 1.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747583660   7 QFAGQPGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAKgDEILARLIT 76
Cdd:cd07110   217 QAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIA-DAFLERLAT 285
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
 18-55 2.46e-03

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: 34.50  E-value: 2.46e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2747583660  18 LEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTC 55
Cdd:cd07132   205 LELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIA 242
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
 9-75 2.82e-03

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: 34.24  E-value: 2.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2747583660   9 AGQPGKILALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTGAkGDEILARLI 75
Cdd:cd07118   218 AARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESI-ADAFVAAVV 283
ALDH_F14-YMR110C cd07135
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ...
 16-76 2.82e-03

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: 34.12  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747583660  16 LALEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTC--------------------ARKLFLPTGAKGDEILARLI 75
Cdd:cd07135   211 VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVApdyvlvdpsvydefveelkkVLDEFYPGGANASPDYTRIV 290


                  .
gi 2747583660  76 T 76
Cdd:cd07135   291 N 291
ALDH_KGSADH-like cd07084
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ...
 18-62 2.92e-03

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: 34.14  E-value: 2.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2747583660  18 LEMGG-NNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLP 62
Cdd:cd07084   206 LELAGfNWKVLGPDAQAVDYVAWQCVQDMTACSGQKCTAQSMLFVP 251
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...
 18-53 4.48e-03

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: 33.73  E-value: 4.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2747583660  18 LEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRC 53
Cdd:cd07099   225 LELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTC 260
PRK13968 PRK13968
putative succinate semialdehyde dehydrogenase; Provisional
 9-64 5.88e-03

putative succinate semialdehyde dehydrogenase; Provisional


Pssm-ID: 184426 [Multi-domain]  Cd Length: 462  Bit Score: 33.30  E-value: 5.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2747583660   9 AGQPGKILALEMGGNNPLIV-KDAEDTLAvVHDIVQSAFISSGQRCTCARKLFLPTG 64
Cdd:PRK13968  224 AGAALKKCVLELGGSDPFIVlNDADLELA-VKAAVAGRYQNTGQVCAAAKRFIIEEG 279
ALDH_F3-13-14_CALDH-like cd07087
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...
 2-53 8.51e-03

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: 32.88  E-value: 8.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2747583660   2 HILheqFAGQP--GKILA-----------LEMGGNNPLIV-KDAeDTLAVVHDIVQSAFISSGQRC 53
Cdd:cd07087   179 HIF---FTGSPavGKIVMeaaakhltpvtLELGGKSPCIVdKDA-NLEVAARRIAWGKFLNAGQTC 240
ALDH_AlkH-like cd07134
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...
 2-76 8.60e-03

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: 32.97  E-value: 8.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747583660   2 HILheqFAGQP--GKI--------LA---LEMGGNNPLIVKDAEDTLAVVHDIVQSAFISSGQRCTCARKLFLPTgAKGD 68
Cdd:cd07134   179 HIF---FTGSPavGKIvmaaaakhLAsvtLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHE-SVKD 254


                  ....*...
gi 2747583660  69 EILARLIT 76
Cdd:cd07134   255 AFVEHLKA 262
 
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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