A9A1B_DANRE
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 03-AUG-2022, entry version 120.
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}.
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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; Q802W2; -.
DR PRIDE; Q802W2; -.
DR Ensembl; ENSDART00000053868; ENSDARP00000053867; ENSDARG00000037061.
DR GeneID; 399481; -.
DR KEGG; dre:399481; -.
DR CTD; 399481; -.
DR ZFIN; ZDB-GENE-040120-5; aldh9a1b.
DR eggNOG; KOG2450; Eukaryota.
DR GeneTree; ENSGT00940000166372; -.
DR HOGENOM; CLU_005391_0_0_1; -.
DR InParanoid; Q802W2; -.
DR OMA; AFTASMH; -.
DR OrthoDB; 538179at2759; -.
DR PhylomeDB; Q802W2; -.
DR TreeFam; TF314257; -.
DR UniPathway; UPA00118; -.
DR PRO; PR:Q802W2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000037061; Expressed in liver and 30 other tissues.
DR ExpressionAtlas; Q802W2; 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..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
