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 16-OCT-2019, entry version 112. 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 Cyprinidae; 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., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA 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., Eliott D., Threadgold G., RA Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., RA Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., RA Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., RA Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., RA Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., RA 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., RA Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., RA Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., RA Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., RA Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., RA Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., RA Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., RA Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human 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; CC EC=1.2.1.47; Evidence={ECO:0000250|UniProtKB:P49189}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + CC NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, CC ChEBI:CHEBI:57540, 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 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 eggNOG; COG1012; LUCA. DR GeneTree; ENSGT00940000166372; -. DR HOGENOM; HOG000271505; -. DR InParanoid; Q802W2; -. DR KO; K00149; -. DR OMA; PKLRGGY; -. DR OrthoDB; 538179at2759; -. DR PhylomeDB; Q802W2; -. DR TreeFam; TF314257; -. DR UniPathway; UPA00118; -. DR PRO; PR:Q802W2; -. DR Proteomes; UP000000437; Chromosome 2. DR Bgee; ENSDARG00000037061; Expressed in 31 organ(s), highest expression level in liver. 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 Complete proteome; Cytoplasm; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 518 4-trimethylaminobutyraldehyde FT dehydrogenase B. FT /FTId=PRO_0000300625. FT NP_BIND 256 260 NAD. {ECO:0000250|UniProtKB:P56533}. FT ACT_SITE 278 278 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU10007}. FT ACT_SITE 312 312 Nucleophile. {ECO:0000255|PROSITE- FT ProRule:PRU10008}. FT BINDING 204 204 NAD. {ECO:0000250|UniProtKB:P56533}. FT BINDING 415 415 NAD. {ECO:0000250|UniProtKB:P56533}. FT CONFLICT 18 20 HPW -> NPG (in Ref. 2; AAH47176). FT {ECO:0000305}. FT CONFLICT 84 84 A -> V (in Ref. 2; AAH47176). FT {ECO:0000305}. FT CONFLICT 87 87 K -> T (in Ref. 2; AAH47176). FT {ECO:0000305}. FT CONFLICT 102 102 L -> M (in Ref. 2; AAH47176). FT {ECO:0000305}. FT CONFLICT 140 140 S -> C (in Ref. 2; AAH47176). FT {ECO:0000305}. FT CONFLICT 167 167 R -> H (in Ref. 2; AAH47176). FT {ECO:0000305}. FT CONFLICT 227 227 E -> D (in Ref. 2; AAH47176). FT {ECO:0000305}. FT CONFLICT 342 342 G -> R (in Ref. 2; AAH47176). FT {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 //