ID   AL9A1_ORYLA             Reviewed;         505 AA.
AC   Q19A30;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   RecName: Full=4-trimethylaminobutyraldehyde dehydrogenase;
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;
DE            EC=1.2.1.3 {ECO:0000250|UniProtKB:P49189};
GN   Name=aldh9A1; Synonyms=aldh9;
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=17236798; DOI=10.1016/j.cbpb.2006.11.006;
RA   Wang X., Zhu S., Khan I.A., Dasmahapatra A.K.;
RT   "Ethanol attenuates Aldh9 mRNA expression in Japanese medaka (Oryzias
RT   latipes) embryogenesis.";
RL   Comp. Biochem. Physiol. 146B:357-363(2007).
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   -!- TISSUE SPECIFICITY: Constitutively expressed in all organs tested:
CC       brain, eye, gill, GI, heart, liver, kidney, muscle, skin, testis and
CC       ovary. {ECO:0000269|PubMed:17236798}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; DQ535181; ABF83193.1; -; mRNA.
DR   RefSeq; NP_001098318.1; NM_001104848.1.
DR   AlphaFoldDB; Q19A30; -.
DR   SMR; Q19A30; -.
DR   STRING; 8090.ENSORLP00000032387; -.
DR   GeneID; 100049493; -.
DR   KEGG; ola:100049493; -.
DR   CTD; 100005587; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   InParanoid; Q19A30; -.
DR   OrthoDB; 2291791at2759; -.
DR   UniPathway; UPA00118; -.
DR   Proteomes; UP000001038; Unplaced.
DR   Proteomes; UP000265180; Chromosome 9.
DR   Proteomes; UP000265200; Chromosome 9.
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..505
FT                   /note="4-trimethylaminobutyraldehyde dehydrogenase"
FT                   /id="PRO_0000300626"
FT   ACT_SITE        265
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        299
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         191
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P56533"
FT   BINDING         243..247
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P56533"
FT   BINDING         402
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P56533"
SQ   SEQUENCE   505 AA;  54482 MW;  2558A9F02C570638 CRC64;
     MSLATLDSMG GASTGSVTVT EQLNFWAGRR VGGRNSEHAE PVFEPATGRV LCQMVPCGAE
     EVDEAIMSAH AAYVQWSKKS GTERARVMLE AARIIRERRE KIAKLEVINN GKSITEALVD
     IDVAWQCIEY YAGVAGTLAG QHFQLPGGAF AYTRREPLGV CVGIGAWNYP FQIAACKSAP
     ALACGNAMVF KPSPFTPVTA VILAEIYKEA GVPDGLFCVV QGGAETGSLL CNHPKVAKVS
     FTGSVPTGKK VMEMSAKGVK QVTLELGGKS PLIIFKDCDL ENAVKGALMA NFLTQGQVCC
     NGTRVFVHKD ILPQFLEEVV KRTKAIAVGD PLLDSTRMGA LITKPHLEKV LGFVRQAKKE
     GGRVLCGGEP FVPSDPKLKG GYFMSPCILD NCRDDMTCVK EEIFGPVMSV LPFDTEEEVI
     RRANNTTFGL ASGVFTRDIS RAHRVAASLE AGTCFINNYN ISPVEVPFGG YKMSGFGREN
     GQVTIEYYSQ LKTVVVETGD VENYF
//