A9A1A_DANRE
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 03-AUG-2022, entry version 126.
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; Q7ZVB2; -.
DR Ensembl; ENSDART00000100283; ENSDARP00000091056; ENSDARG00000069100.
DR Ensembl; ENSDART00000137838; ENSDARP00000118280; ENSDARG00000069100.
DR Ensembl; ENSDART00000171771; ENSDARP00000134258; ENSDARG00000069100.
DR Ensembl; ENSDART00000182650; ENSDARP00000152850; ENSDARG00000114905.
DR GeneID; 100005587; -.
DR KEGG; dre:100005587; -.
DR CTD; 100005587; -.
DR ZFIN; ZDB-GENE-030131-1257; aldh9a1a.1.
DR eggNOG; KOG2450; Eukaryota.
DR GeneTree; ENSGT00940000163309; -.
DR HOGENOM; CLU_005391_0_0_1; -.
DR InParanoid; Q7ZVB2; -.
DR OrthoDB; 538179at2759; -.
DR PhylomeDB; Q7ZVB2; -.
DR TreeFam; TF314257; -.
DR Reactome; R-DRE-71262; Carnitine synthesis.
DR UniPathway; UPA00118; -.
DR PRO; PR:Q7ZVB2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 8.
DR Bgee; ENSDARG00000069100; Expressed in intestine and 29 other 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:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
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 Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 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 Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 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
