ID A0A084QG60_STAC4 Unreviewed; 509 AA.
AC A0A084QG60;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=4-trimethylaminobutyraldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00040275};
DE EC=1.2.1.19 {ECO:0000256|ARBA:ARBA00039138};
DE EC=1.2.1.46 {ECO:0000256|ARBA:ARBA00044057};
DE EC=1.2.1.47 {ECO:0000256|ARBA:ARBA00039125};
DE AltName: Full=Aldehyde dehydrogenase family 9 member A1 {ECO:0000256|ARBA:ARBA00041858};
DE AltName: Full=Formaldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00044324};
DE AltName: Full=Gamma-aminobutyraldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00044302};
GN ORFNames=S40285_04362 {ECO:0000313|EMBL:KFA62945.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA62945.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA62945.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA62945.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
CC -!- FUNCTION: Converts gamma-trimethylaminobutyraldehyde into gamma-
CC butyrobetaine with high efficiency (in vitro). Can catalyze the
CC irreversible oxidation of a broad range of aldehydes to the
CC corresponding acids in an NAD-dependent reaction, but with low
CC efficiency. Catalyzes the oxidation of aldehydes arising from biogenic
CC amines and polyamines. {ECO:0000256|ARBA:ARBA00043882}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5-hydroxyindol-3-yl)acetaldehyde + H2O + NAD(+) = (5-
CC hydroxyindol-3-yl)acetate + 2 H(+) + NADH; Xref=Rhea:RHEA:31215,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:50157,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62622;
CC Evidence={ECO:0000256|ARBA:ARBA00043724};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxyphenylacetaldehyde + H2O + NAD(+) = 3,4-
CC dihydroxyphenylacetate + 2 H(+) + NADH; Xref=Rhea:RHEA:69080,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17612,
CC ChEBI:CHEBI:27978, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000256|ARBA:ARBA00043811};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-(trimethylamino)butanal + H2O + NAD(+) = 4-
CC (trimethylamino)butanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:17985,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16244,
CC ChEBI:CHEBI:18020, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.47;
CC Evidence={ECO:0000256|ARBA:ARBA00036400};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264,
CC ChEBI:CHEBI:59888; EC=1.2.1.19;
CC Evidence={ECO:0000256|ARBA:ARBA00043799};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + pentanal = 2 H(+) + NADH + pentanoate;
CC Xref=Rhea:RHEA:69092, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31011, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:84069; Evidence={ECO:0000256|ARBA:ARBA00043741};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + propanal = 2 H(+) + NADH + propanoate;
CC Xref=Rhea:RHEA:67256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17153, ChEBI:CHEBI:17272, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00043823};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + spermine monoaldehyde = 2 H(+) + N-(2-
CC carboxyethyl)spermidine + NADH; Xref=Rhea:RHEA:69168,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:180903, ChEBI:CHEBI:180913;
CC Evidence={ECO:0000256|ARBA:ARBA00043708};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH;
CC Xref=Rhea:RHEA:67276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:88528; Evidence={ECO:0000256|ARBA:ARBA00043662};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + imidazole-4-acetaldehyde + NAD(+) = 2 H(+) + imidazole-
CC 4-acetate + NADH; Xref=Rhea:RHEA:31059, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27398, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:57969;
CC Evidence={ECO:0000256|ARBA:ARBA00043820};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:25294, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00043790};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acrolein + H2O + NAD(+) = acrylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:69084, ChEBI:CHEBI:15368, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:37080, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00043666};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00024149};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanal + H2O + NAD(+) = butanoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:69088, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15743, ChEBI:CHEBI:17968, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00043754};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formaldehyde + H2O + NAD(+) = formate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16425, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16842, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.46;
CC Evidence={ECO:0000256|ARBA:ARBA00043759};
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; KL660772; KFA62945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084QG60; -.
DR STRING; 1283841.A0A084QG60; -.
DR HOGENOM; CLU_005391_0_0_1; -.
DR InParanoid; A0A084QG60; -.
DR OMA; CREGIRM; -.
DR OrthoDB; 2291791at2759; -.
DR Proteomes; UP000028524; Unassembled WGS sequence.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR11699:SF228; 4-TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000028524}.
FT DOMAIN 21..492
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 254
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 509 AA; 54264 MW; 7DCECDD6F8DB7213 CRC64;
MTFSKEIHTF HSGRPQPESS SSSNTFTSVD PATAKPLATI YTTTPTQLND AIASAHAAFP
AWSQTPPARR AQILLRAAAI LRERNDLLAK TETLDTGKPL SETSTVDIVT GADVLEYYAQ
YVASGIPGQN TRLRSDAFVL TSKEPLGVCA GIGAWNYPMQ IALWKSAPCL AAGNCMVYKP
SEVTPLHANT LAQIYIEAGV PPGVFNVVFG DGVSVGAPLV AHSGIAKVSF TGQVSTGSKV
ASEAAKGMKG ITMELGGKSP LVILPDADVD EAADVAMVAN FFSTGQVCTN GTRVFVPDTL
LERVEAALVR RCQAGIRMGH PIDPDTNLGP VVSATHRDKV NMYIKHGRDI DRAKVLYDGT
AVPLKASLSK DGFWVPPVIF TNCTDSMRVA REEIFGPVMC ILPYQTKGRP QEEWLPELIR
RANDTPMGLA AGVVSSDVGL AQDVIRQLEA GITWINTWGE SPAEMPVGGW KMSGIGLENG
HEGIQAYLRT KSTLVQLGKG ACQGVFAKL
//
