ID E9QH31_DANRE Unreviewed; 490 AA. AC E9QH31; A0A8M1P3N5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 2. DT 02-OCT-2024, entry version 79. DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492}; GN Name=aldh3a2b {ECO:0000313|Ensembl:ENSDARP00000103212, GN ECO:0000313|RefSeq:NP_001315147.1, GN ECO:0000313|ZFIN:ZDB-GENE-040912-103}; GN Synonyms=zgc:103715 {ECO:0000313|RefSeq:NP_001315147.1}; 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 {ECO:0000313|Ensembl:ENSDARP00000103212}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000103212} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000103212}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [2] {ECO:0000313|RefSeq:NP_001315147.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001315147.1}; RX PubMed=22840776; RA Zhou L., Ishizaki H., Spitzer M., Taylor K.L., Temperley N.D., RA Johnson S.L., Brear P., Gautier P., Zeng Z., Mitchell A., Narayan V., RA McNeil E.M., Melton D.W., Smith T.K., Tyers M., Westwood N.J., Patton E.E.; RT "ALDH2 mediates 5-nitrofuran activity in multiple species."; RL Chem. Biol. 19:883-892(2012). RN [3] {ECO:0000313|Ensembl:ENSDARP00000103212, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000103212}; RX PubMed=23594743; DOI=10.1038/nature12111; RG Genome Reference Consortium Zebrafish; 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., Eliott D., RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B., RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D., RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., RA Berger A., 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., Lanz C., Raddatz G., Osoegawa K., Zhu B., RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., RA 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 [4] {ECO:0000313|RefSeq:NP_001315147.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001315147.1}; RX PubMed=26469318; RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M., RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D., RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E., RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M., RA Reith W., Hertzano R.; RT "RFX transcription factors are essential for hearing in mice."; RL Nat. Commun. 6:8549-8549(2015). RN [5] {ECO:0000313|RefSeq:NP_001315147.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001315147.1}; RX PubMed=27189481; RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I., RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y., RA Bobe J.; RT "Gene evolution and gene expression after whole genome duplication in fish: RT the PhyloFish database."; RL BMC Genomics 17:368-368(2016). RN [6] {ECO:0000313|RefSeq:NP_001315147.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001315147.1}; RX PubMed=27357367; RA Loncar J., Popovic M., Krznar P., Zaja R., Smital T.; RT "The first characterization of multidrug and toxin extrusion (MATE/SLC47) RT proteins in zebrafish (Danio rerio)."; RL Sci. Rep. 6:28937-28937(2016). RN [7] {ECO:0000313|RefSeq:NP_001315147.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001315147.1}; RX PubMed=28252024; RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A., RA Choudhary J.S., Emes R.D., Grant S.G.; RT "Evolution of complexity in the zebrafish synapse proteome."; RL Nat. Commun. 8:14613-14613(2017). RN [8] {ECO:0000313|RefSeq:NP_001315147.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001315147.1}; RG RefSeq; RL Submitted (JUN-2024) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-hexadecenal + H2O + NAD(+) = (E)-hexadec-2-enoate + 2 CC H(+) + NADH; Xref=Rhea:RHEA:36135, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17585, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:72745; CC Evidence={ECO:0000256|ARBA:ARBA00035777}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesal + H2O + NAD(+) = (2E,6E)-farnesoate + 2 H(+) CC + NADH; Xref=Rhea:RHEA:24216, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15894, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:83276; EC=1.2.1.94; CC Evidence={ECO:0000256|ARBA:ARBA00036228}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 H(+) + hexadecanoate + NADH = H2O + hexadecanal + NAD(+); CC Xref=Rhea:RHEA:33739, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17600, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00035953}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2,6,10,14-tetramethylpentadecanal + H2O + NAD(+) = 2,6,10,14- CC tetramethylpentadecanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:44016, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:49189, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:77268; CC Evidence={ECO:0000256|ARBA:ARBA00035974}; CC -!- CATALYTIC ACTIVITY: CC Reaction=22-oxodocosanoate + H2O + NAD(+) = docosanedioate + 2 H(+) + CC NADH; Xref=Rhea:RHEA:39015, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:76298, CC ChEBI:CHEBI:76299; Evidence={ECO:0000256|ARBA:ARBA00036932}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + NAD(+) + octadecanal = 2 H(+) + NADH + octadecanoate; CC Xref=Rhea:RHEA:44020, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17034, ChEBI:CHEBI:25629, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00035984}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + NAD(+) + octanal = 2 H(+) + NADH + octanoate; CC Xref=Rhea:RHEA:44100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00000589}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + NAD(+) + tetradecanal = 2 H(+) + NADH + tetradecanoate; CC Xref=Rhea:RHEA:44172, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:84067; Evidence={ECO:0000256|ARBA:ARBA00035786}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + heptanal + NAD(+) = 2 H(+) + heptanoate + NADH; CC Xref=Rhea:RHEA:44108, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:32362, ChEBI:CHEBI:34787, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00036881}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a fatty aldehyde + H2O + NAD(+) = a fatty acid + 2 H(+) + CC NADH; Xref=Rhea:RHEA:49832, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28868, ChEBI:CHEBI:35746, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00036717}; 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:0000256|ARBA:ARBA00024149}; CC -!- CATALYTIC ACTIVITY: CC Reaction=decanal + H2O + NAD(+) = decanoate + 2 H(+) + NADH; CC Xref=Rhea:RHEA:44104, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:27689, ChEBI:CHEBI:31457, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00036332}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dodecanoate + 2 H(+) + NADH = dodecanal + H2O + NAD(+); CC Xref=Rhea:RHEA:44168, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:18262, ChEBI:CHEBI:27836, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00036265}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004131}; Single-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004131}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004131}. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492, CC ECO:0000256|RuleBase:RU003345}. 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; CU463284; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001315147.1; NM_001328218.1. DR STRING; 7955.ENSDARP00000103212; -. DR PaxDb; 7955-ENSDARP00000103212; -. DR Ensembl; ENSDART00000114885.5; ENSDARP00000103212.4; ENSDARG00000029381.9. DR GeneID; 447920; -. DR KEGG; dre:447920; -. DR AGR; ZFIN:ZDB-GENE-040912-103; -. DR CTD; 447920; -. DR ZFIN; ZDB-GENE-040912-103; aldh3a2b. DR eggNOG; KOG2456; Eukaryota. DR HOGENOM; CLU_005391_3_0_1; -. DR OMA; DHIPRIR; -. DR OrthoDB; 606537at2759; -. DR PhylomeDB; E9QH31; -. DR TreeFam; TF314264; -. DR Proteomes; UP000000437; Chromosome 21. DR Bgee; ENSDARG00000029381; Expressed in intestine and 20 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; IBA:GO_Central. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central. DR GO; GO:0006081; P:cellular aldehyde metabolic process; IBA:GO_Central. DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW. DR CDD; cd07132; ALDH_F3AB; 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 InterPro; IPR012394; Aldehyde_DH_NAD(P). DR PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1. DR PANTHER; PTHR43570:SF9; ALDEHYDE DEHYDROGENASE FAMILY 3 MEMBER A2; 1. DR Pfam; PF00171; Aldedh; 1. DR PIRSF; PIRSF036492; ALDH; 1. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 1: Evidence at protein level; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Microsome {ECO:0000256|ARBA:ARBA00022848}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR036492, KW ECO:0000256|RuleBase:RU003345}; KW Proteomics identification {ECO:0007829|PeptideAtlas:E9QH31}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 470..488 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 5..426 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT ACT_SITE 210 FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1, FT ECO:0000256|PROSITE-ProRule:PRU10007" FT ACT_SITE 244 FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1" SQ SEQUENCE 490 AA; 55060 MW; 081558B1890338EF CRC64; MSREQKAVER ARKAFFTGRS KSLEYRISQL KNLQRFMQER QKEIAEALKK DLKRSEFGTS LYETLGVESE INLALKKLKE WAAPRPVNKS LMTISDQVYI QPEPLGVVLI IGAWNYPWAV TVGPLVGAIA AGNAAVIKPS EVSAHTSKVM EEFLPLYLDK ELYPVVTGGV KETQELLKQR FDHIFYTGNG MVGKIIMEAA AKHLTPTTLE LGGKSPCYID KDCDLTIACR RIAWGKYSNC GQTCIAPDYI LCDPSIQDRV IEEIKKNIKE FYTENPQKCP DYGRIINQRH FKRLMSLMEG SSIAVSGEHN EAECYIAPTV LRDVKPDAKV MQEEIFGPLL PIVTVNSVDE AIKFINQRDK PLALYIFSSD KKLIDRMIAE TSSGGLMAND CLMHFSVSSL PFGGVGDSGM GRYHGKHGFD NLSHMRGVLL KQLKMEAVNK MRYPPHTADK LGWARFFIVR HVDFGSLGRM AMLALMVVFA AVIIQKYFTD //