ID A0A493T008_ANAPP Unreviewed; 488 AA. AC A0A493T008; DT 05-JUN-2019, integrated into UniProtKB/TrEMBL. DT 05-JUN-2019, sequence version 1. DT 29-MAY-2024, entry version 19. DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492}; OS Anas platyrhynchos platyrhynchos (Northern mallard). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae; OC Anatinae; Anas. OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000019234.1, ECO:0000313|Proteomes:UP000016666}; RN [1] {ECO:0000313|Ensembl:ENSAPLP00000019234.1, ECO:0000313|Proteomes:UP000016666} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.; RT "A new Pekin duck reference genome."; RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSAPLP00000019234.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2023) 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 AlphaFoldDB; A0A493T008; -. DR Ensembl; ENSAPLT00000026106.1; ENSAPLP00000019234.1; ENSAPLG00000002714.2. DR GeneTree; ENSGT00940000157944; -. DR OMA; AVANCIV; -. DR Proteomes; UP000016666; Chromosome 20. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; IEA:TreeGrafter. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:TreeGrafter. DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro. 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 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; 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 Reference proteome {ECO:0000313|Proteomes:UP000016666}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 465..487 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 3..425 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT COILED 23..50 FT /evidence="ECO:0000256|SAM:Coils" 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 488 AA; 54249 MW; F0E9B29C0215E36D CRC64; MERMQQVVGR ARAAFSSGRC RSLEFRLQQL KNLERMVREK EKEILAALQS DLHKCGHNAY SHEVMGVLGE LAQAMENLPS WAAPQPVKKN LLTMRDEAYI YPEPLGVVLV IGAWNYPFML VVQPLIGAIA AGNAVVVKPS EVSEHTSQLL ADLLPQYLDE ELYPVVTGGV PETTELLKQR FDHILYTGNT AVGKIVMAAA AKHLTPVTLE LGGKSPCYID KDCDLAVACR RITWGKYMNC GQTCIAPDYI LCEPSIQSQV VENIKATLQE FYGEDVKKSP DYERIVNKRH FRRIVSLLEG QKIAHGGETD EASCFIAPTI LTDVSAESKV MEEEIFGPVL PIVSVKGVDE AIEFINSREK PLALYVFSND KKLIKRVISE TSSGGMTAND VLMHSTVLDL PFGGVGNSGM GAYHGKHSFE TFSHHRACLI KDLKMEGMNK LRYPPGSQKK LDWAKFFILK RFDKVRYGLI FLALLGVVAA VMIKVMFP //