AL9A1_ORYLA
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 03-AUG-2022, entry version 83.
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.ENSORLP00000017772; -.
DR PRIDE; Q19A30; -.
DR GeneID; 100049493; -.
DR KEGG; ola:100049493; -.
DR CTD; 100005587; -.
DR eggNOG; KOG2450; Eukaryota.
DR InParanoid; Q19A30; -.
DR OrthoDB; 538179at2759; -.
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: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..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
