ID   A9A1A_DANRE             Reviewed;         508 AA.
AC   Q7ZVB2; Q6NYB3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=4-trimethylaminobutyraldehyde dehydrogenase A;
DE            Short=TMABA-DH;
DE            Short=TMABADH;
DE            EC=1.2.1.47 {ECO:0000250|UniProtKB:P49189};
DE   AltName: Full=Aldehyde dehydrogenase family 9 member A1-A;
DE            EC=1.2.1.3 {ECO:0000250|UniProtKB:P49189};
GN   Name=aldh9a1a; Synonyms=aldh9a1l;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250|UniProtKB:P49189}.
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:0000250|UniProtKB:P49189};
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:0000250|UniProtKB:P49189};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis.
CC       {ECO:0000250|UniProtKB:P49189}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P49189}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9JLJ3}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; BC045932; AAH45932.1; -; mRNA.
DR   EMBL; BC066668; AAH66668.1; -; mRNA.
DR   RefSeq; NP_958879.1; NM_201471.1.
DR   RefSeq; XP_005166831.1; XM_005166774.2.
DR   AlphaFoldDB; Q7ZVB2; -.
DR   SMR; Q7ZVB2; -.
DR   STRING; 7955.ENSDARP00000091056; -.
DR   PaxDb; 7955-ENSDARP00000091056; -.
DR   GeneID; 100005587; -.
DR   KEGG; dre:100005587; -.
DR   AGR; ZFIN:ZDB-GENE-030131-1257; -.
DR   CTD; 100005587; -.
DR   ZFIN; ZDB-GENE-030131-1257; aldh9a1a.1.
DR   eggNOG; KOG2450; Eukaryota.
DR   HOGENOM; CLU_005391_0_0_1; -.
DR   InParanoid; Q7ZVB2; -.
DR   OMA; GDHTSYV; -.
DR   OrthoDB; 2291791at2759; -.
DR   PhylomeDB; Q7ZVB2; -.
DR   TreeFam; TF314257; -.
DR   Reactome; R-DRE-71262; Carnitine synthesis.
DR   UniPathway; UPA00118; -.
DR   PRO; PR:Q7ZVB2; -.
DR   Proteomes; UP000000437; Alternate scaffold 8.
DR   Proteomes; UP000000437; Chromosome 8.
DR   Bgee; ENSDARG00000069100; Expressed in intestine and 29 other cell types or tissues.
DR   ExpressionAtlas; Q7ZVB2; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0047105; F:4-trimethylammoniobutyraldehyde dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0045329; P:carnitine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; ISS:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR   CDD; cd07090; ALDH_F9_TMBADH; 1.
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:SF232; 4-TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE A-RELATED; 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   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..508
FT                   /note="4-trimethylaminobutyraldehyde dehydrogenase A"
FT                   /id="PRO_0000300624"
FT   ACT_SITE        268
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        302
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         194
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P56533"
FT   BINDING         246..250
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P56533"
FT   BINDING         405
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P56533"
FT   CONFLICT        61
FT                   /note="G -> V (in Ref. 1; AAH66668)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   508 AA;  55262 MW;  5290ABC5F72553B2 CRC64;
     MAQQPLLSLP EFQSVSTGTL VVKEPLNFWG GARVKPRDTK NSEPVYEPAT GRVLCDMIPC
     GEEEVDQAIK SAHSAYLKWS QLSGMERSRI MLEAARIIRE RRNAIAKAEV ANNGKSITEA
     EVDIDVAWQC IEYYAGIAPT LSGQHIQLPG GSFAYTRREP LGVCVGIGAW NYPFQIAAWK
     SAPALACGNA MVFKPSPMTP VTAVMLAEIY KEAGVPDGLF NVVQGGAETG SLLCHHPMVA
     KVSFTGSVPT GKKVMEMAAK SVKQVTLELG GKSPLIIFKD CELENAIKGA LMANFLTQGE
     VCCNGTRVFV QREIMPKFLE EVVKRTKAIS VGDPLCEGTR MGALISKPHM EKVLGFIKQA
     KEQGGKVLCG GERFVPNDPK LKDGYFVSPC VLDNCRDDMT CVKEEIFGPV MSVLPFDTEE
     EVLQRANNTT FGLASGVFTR DIARAHRVAA NLQAGTCYIN NYNVGPVEVP FGGYKMSGFG
     RENGTVTIEY YSQLKTVVVE MGDVESLF
//