ID   A9A1B_DANRE             Reviewed;         518 AA.
AC   Q802W2; A2AWD6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=4-trimethylaminobutyraldehyde dehydrogenase B;
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-B;
DE            EC=1.2.1.3 {ECO:0000250|UniProtKB:P49189};
GN   Name=aldh9a1b; Synonyms=aldh9a1; ORFNames=si:ch211-284b7.5;
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 GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (FEB-2003) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL954171; CAM14219.1; -; Genomic_DNA.
DR   EMBL; BC047176; AAH47176.1; -; mRNA.
DR   RefSeq; NP_958916.1; NM_201508.1.
DR   RefSeq; XP_005163288.1; XM_005163231.3.
DR   AlphaFoldDB; Q802W2; -.
DR   SMR; Q802W2; -.
DR   STRING; 7955.ENSDARP00000053867; -.
DR   PaxDb; 7955-ENSDARP00000053867; -.
DR   GeneID; 399481; -.
DR   KEGG; dre:399481; -.
DR   AGR; ZFIN:ZDB-GENE-040120-5; -.
DR   CTD; 399481; -.
DR   ZFIN; ZDB-GENE-040120-5; aldh9a1b.
DR   eggNOG; KOG2450; Eukaryota.
DR   HOGENOM; CLU_005391_0_0_1; -.
DR   InParanoid; Q802W2; -.
DR   OMA; EFYAGAC; -.
DR   OrthoDB; 2291791at2759; -.
DR   PhylomeDB; Q802W2; -.
DR   TreeFam; TF314257; -.
DR   UniPathway; UPA00118; -.
DR   PRO; PR:Q802W2; -.
DR   Proteomes; UP000000437; Chromosome 2.
DR   Bgee; ENSDARG00000037061; Expressed in liver and 30 other cell types or tissues.
DR   ExpressionAtlas; Q802W2; baseline.
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:SF132; 4-TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE B; 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..518
FT                   /note="4-trimethylaminobutyraldehyde dehydrogenase B"
FT                   /id="PRO_0000300625"
FT   ACT_SITE        278
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        312
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         204
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P56533"
FT   BINDING         256..260
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P56533"
FT   BINDING         415
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P56533"
FT   CONFLICT        18..20
FT                   /note="HPW -> NPG (in Ref. 2; AAH47176)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        84
FT                   /note="A -> V (in Ref. 2; AAH47176)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="K -> T (in Ref. 2; AAH47176)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        102
FT                   /note="L -> M (in Ref. 2; AAH47176)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        140
FT                   /note="S -> C (in Ref. 2; AAH47176)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167
FT                   /note="R -> H (in Ref. 2; AAH47176)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        227
FT                   /note="E -> D (in Ref. 2; AAH47176)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        342
FT                   /note="G -> R (in Ref. 2; AAH47176)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   518 AA;  56438 MW;  105AB1667E4199FF CRC64;
     MALMRCLLPP GFYRTLYHPW TRCASSGTLQ IKDPLNFWCG ARVDLKDVKT KSEPVFEPAT
     GRVLCRLQTC GSAEVDAAVR NASAAFKVWR KLSGMERARV MLEAARLIEK RREEIAEMEV
     INNGKSITEA RLDVDSARLS IEYFAGQATT LSGQHVQLPG GSFAYTRREP FGVCVGIGAW
     NYPFQIAAWK SAPAIACGNS MVFKPSPLTP VTAVLLAEIY RQAGAPEGLF NVVQGGQETG
     SLLCLHPSVE KVSFTGSVPT GKKIMEMASR GVKAVTLELG GKSPLIIFED TDLENAVRGA
     LMANFLSQGQ VCSNGTRVFV QSSIVPQFLK EVVRRTKAIS IGDPLLDETR MGALVSKAHL
     DKVLRYVEQA KNEGAQVLCG GEPFSPADPK LKDGYYMTPC VLDSCTDDMT CVKEEIFGPV
     MSVLTFDTED EVLRRANDSD LGLAAGVFTK DVKRAHRVIE NLQAGSCFIN NYNITPVEVP
     FGGFKASGIG RENGQVTIEF YSQLKTVVVE MGDVDSLF
//