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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSITVQTQ 79
Cdd:cd07090   386 YGLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEMG 457

betaine aldehyde dehydrogenase; Provisional

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSITVQTQ 79
Cdd:PRK13252  411 YGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVEMG 482

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSITVQTQ 79
Cdd:cd07090   386 YGLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEMG 457

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSITV 76
Cdd:cd07091   408 YGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQY-FNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSITV 76
Cdd:cd07078   363 YGLAAGVFTRDLERALRVAERLEAGTVWINDYsVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSITV 76
Cdd:cd07141   412 YGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480

betaine aldehyde dehydrogenase; Provisional

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSITVQTQ 79
Cdd:PRK13252  411 YGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVEMG 482

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSITV 76
Cdd:cd07093   387 YGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1499194631   3 VDSCAYGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSITVQ 77
Cdd:cd07107   381 ANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVR 455

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQYfNLNRG--APFGGVKESGIGREYCHDTLNHYSHVKSITV 76
Cdd:cd06534   298 YGLTAGVFTRDLNRALRVAERLRAGTVYINDS-SIGVGpeAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499194631   7 AYGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSITV 76
Cdd:cd07115   382 EYGLAAGVWTRDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWV 451

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGREYCHDT-LNHYSHVKSITV 76
Cdd:cd07108   388 YGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTVNI 457

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSITVQ 77
Cdd:cd07140   416 YGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIE 485

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1499194631   4 DSCaYGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSITV 76
Cdd:cd07144   411 DTT-YGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSITV 76
Cdd:cd07116   409 YGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 477

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1499194631   6 CAYGLASGIYTSNLANAMKTADLLEAGNVWIN-QYFNLnrGAPFGGVKESGIGREYCHDTLNHYSHVKSIT 75
Cdd:cd07138   397 TPYGLAGYVWSADPERARAVARRLRAGQVHINgAAFNP--GAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1499194631   3 VDSCAYGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLnR--GAPFGGVKESGIGRE 59
Cdd:cd07149   379 ANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDSSTF-RvdHMPYGGVKESGTGRE 436

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGA-PFGGVKESGIGREYCHDTLNHYSHVKSITV 76
Cdd:cd07145   387 YGLQASVFTNDINRALKVARELEAGGVVINDSTRFRWDNlPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1499194631   4 DSCaYGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSITV 76
Cdd:cd07120   384 DTD-YGLAASVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGRE 59
Cdd:cd07100   361 FGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPFGGVKRSGYGRE 412

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499194631   1 MPVDS----------CAYGLASGIYTSNLANAMKTADLLEAGNVWINQ--YFNLNRGAPFGGVKESGIGREYCHDTLNHY 68
Cdd:cd07099   366 MPVADedeaialandSRYGLSASVFSRDLARAEAIARRLEAGAVSINDvlLTAGIPALPFGGVKDSGGGRRHGAEGLREF 445

                  ....*...
gi 1499194631  69 SHVKSITV 76
Cdd:cd07099   446 CRPKAIAR 453

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWIN-QYFNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSITV 76
Cdd:cd07104   362 YGLSAAVFTRDLERAMAFAERLETGMVHINdQTVNDEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499194631   3 VDSCAYGLASGIYTSNLANAMKTADLLEAGNVWINqyfnlnrG--------APFGGVKESGIGREYCHDTLNHYSHVKSI 74
Cdd:cd07105   358 ANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN-------GmtvhdeptLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430

                  ..
gi 1499194631  75 TV 76
Cdd:cd07105   431 TI 432

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1499194631   3 VDSCAYGLASGIYTSNLANAMKTADLLEAGNVWINQY--FNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSITV 76
Cdd:cd07098   388 ANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFgvNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463

aminobutyraldehyde dehydrogenase;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1499194631   6 CAYGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSI 74
Cdd:PRK13473  402 SDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQYfnLNRGA---PFGGVKESGIGREYCHDTLNHYSHVKSI 74
Cdd:cd07082   403 YGLQASIFTKDINKARKLADALEVGTVNINSK--CQRGPdhfPFLGRKDSGIGTQGIGDALRSMTRRKGI 470

putative succinate semialdehyde dehydrogenase; Provisional

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSI 74
Cdd:PRK13968  391 FGLSATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1499194631   3 VDSCAYGLASGIYTSNLANAMKTADLLEAG--NVWINQYFNLNRgAPFGGVKESGIG-REYCHDTLNHYSHVKSITV 76
Cdd:cd07146   376 SNSTAYGLSSGVCTNDLDTIKRLVERLDVGtvNVNEVPGFRSEL-SPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451

betaine aldehyde dehydrogenase

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSIT 75
Cdd:PLN02467  419 YGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQVT 486

NADP-dependent succinate-semialdehyde dehydrogenase I;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGRE 59
Cdd:PRK11241  412 FGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGRE 463

succinic semialdehyde dehydrogenase; Reviewed

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWINQYFNL---NRGAPFGGVKESGIGREYCHDTLNHYSHVKSITVQ 77
Cdd:PRK09407  419 YGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAawgSVDAPMGGMKDSGLGRRHGAEGLLKYTESQTIATQ 491

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).

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1499194631   8 YGLASGIYTSNLANAMK--TADLLEAGNVWINqyfNLNRGA----PFGGVKESGIGREYCHDTLNHYSHVKSITV 76
Cdd:cd07086   404 QGLSSSIFTEDLREAFRwlGPKGSDCGIVNVN---IPTSGAeiggAFGGEKETGGGRESGSDAWKQYMRRSTCTI 475

succinic semialdehyde dehydrogenase; Reviewed

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1499194631   7 AYGLASGIYTSNLANAMKTADLLEAGNVWINQYFNLNRGAPFGGVKESGIGRE 59
Cdd:PRK09406  387 TFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRE 439

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1499194631   5 SCAYGLASGIYTSNLANAMKTADLLEAGNVwinqYFNLN-RGA-----PFGGVKESGIGREYC-HDTLNHYSHVKSIT 75
Cdd:cd07124   436 DTEYGLTGGVFSRSPEHLERARREFEVGNL----YANRKiTGAlvgrqPFGGFKMSGTGSKAGgPDYLLQFMQPKTVT 509

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVWInqyfnlNR---GA-----PFGGVKESGIG 57
Cdd:cd07125   435 YGLTLGIHSRDEREIEYWRERVEAGNLYI------NRnitGAivgrqPFGGWGLSGTG 486

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499194631   3 VDSCAYGLASGIYTSNLANAMKTADLLEAGNVWINQYfnlNRGA-----PFGGVKESGIG 57
Cdd:cd07083   422 ANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRK---ITGAlvgvqPFGGFKLSGTN 478

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1499194631  10 LASGIYTSNLANAMKTADLLEAGNVWIN----QYfnLNRGAPFGGVKESGIGREYCHDTLNHYSHVKSI 74
Cdd:cd07137   364 LAAYVFTKNKELKRRIVAETSSGGVTFNdtvvQY--AIDTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430

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.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1499194631  47 PFGGVKESGIGR---EYCHDTlnhYSHVKSITVQT 78
Cdd:cd07136   397 PFGGVGNSGMGSyhgKYSFDT---FSHKKSILKKS 428

1-pyrroline-5-carboxylate dehydrogenase; Provisional

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1499194631   8 YGLASGIYTSNLANAMKTADLLEAGNVwinqYFNLN-RGA-----PFGGVKESGI-----GREYchdtLNHYSHVKSIT 75
Cdd:PRK03137  441 YGLTGAVISNNREHLEKARREFHVGNL----YFNRGcTGAivgyhPFGGFNMSGTdskagGPDY----LLLFLQAKTVS 511

aldehyde dehydrogenase

                          10        20
                  ....*....|....*....|....*....
gi 1499194631  47 PFGGVKESGIGREYCHDTLNHYSHVKSIT 75
Cdd:PLN02203  413 PFGGVGESGFGRYHGKYSFDTFSHEKAVL 441

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1499194631   7 AYGLASGIYTSNLANAMKTADLLEAGNVwinqyfNLNR---GA----PFGGVKESGIGR-------EYC 61
Cdd:cd07095   362 RFGLSAGLLSDDEALFERFLARIRAGIV------NWNRpttGAsstaPFGGVGLSGNHRpsayyaaDYC 424