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Database: UniProt
Entry: A0A364N908_9PLEO
LinkDB: A0A364N908_9PLEO
Original site: A0A364N908_9PLEO 
ID   A0A364N908_9PLEO        Unreviewed;       341 AA.
AC   A0A364N908;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Very-long-chain 3-oxoacyl-CoA reductase {ECO:0000256|HAMAP-Rule:MF_03107};
DE            EC=1.1.1.330 {ECO:0000256|HAMAP-Rule:MF_03107};
DE   AltName: Full=3-ketoacyl-CoA reductase {ECO:0000256|HAMAP-Rule:MF_03107};
DE            Short=3-ketoreductase {ECO:0000256|HAMAP-Rule:MF_03107};
DE            Short=KAR {ECO:0000256|HAMAP-Rule:MF_03107};
DE   AltName: Full=Microsomal beta-keto-reductase {ECO:0000256|HAMAP-Rule:MF_03107};
GN   ORFNames=DDE83_002931 {ECO:0000313|EMBL:RAR13746.1};
OS   Stemphylium lycopersici.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Stemphylium.
OX   NCBI_TaxID=183478 {ECO:0000313|EMBL:RAR13746.1, ECO:0000313|Proteomes:UP000249619};
RN   [1] {ECO:0000313|Proteomes:UP000249619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIDEFI 213 {ECO:0000313|Proteomes:UP000249619};
RA   Medina R., Franco M.E.E., Lucentini C.G., Saparrat M.C.N., Balatti P.A.;
RT   "Draft genome sequence of Stemphylium lycopersici strain CIDEFI 213.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the microsomal membrane bound fatty acid
CC       elongation system, which produces the 26-carbon very long-chain fatty
CC       acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-
CC       ketoacyl-CoA intermediate that is formed in each cycle of fatty acid
CC       elongation. VLCFAs serve as precursors for ceramide and sphingolipids.
CC       {ECO:0000256|HAMAP-Rule:MF_03107}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-
CC         long-chain 3-oxoacyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:48680,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:85440, ChEBI:CHEBI:90725; EC=1.1.1.330;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03107};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|HAMAP-Rule:MF_03107}; Single-pass membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_03107}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|HAMAP-
CC       Rule:MF_03107}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RAR13746.1}.
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DR   EMBL; QGDH01000031; RAR13746.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A364N908; -.
DR   STRING; 183478.A0A364N908; -.
DR   OrthoDB; 6845at2759; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000249619; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045703; F:ketoreductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0141040; F:very-long-chain 3-oxoacyl-CoA reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030497; P:fatty acid elongation; IEA:UniProtKB-UniRule.
DR   CDD; cd05356; 17beta-HSD1_like_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_03107; 3_ketoreductase; 1.
DR   InterPro; IPR027533; 3_ketoreductase_fungal.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43086:SF2; HYDROXYSTEROID DEHYDROGENASE-LIKE PROTEIN 1; 1.
DR   PANTHER; PTHR43086; VERY-LONG-CHAIN 3-OXOOACYL-COA REDUCTASE; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PIRSF; PIRSF000126; 11-beta-HSD1; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP-
KW   Rule:MF_03107};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW   Rule:MF_03107};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW   Rule:MF_03107};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_03107};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_03107};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03107};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_03107};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_03107}; Reference proteome {ECO:0000313|Proteomes:UP000249619};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_03107};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_03107}.
FT   TRANSMEM        21..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        217
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03107"
FT   BINDING         204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03107"
SQ   SEQUENCE   341 AA;  36869 MW;  D31D8EB612E5F61A CRC64;
     MASIMETFGV RIDASNSLVQ AAVYGFLLVG IASFAAPVAS TIRVLLSLFV LPGKSLSTFG
     PRGTWALITG ASDGIGKEFA LSFAAKGYNL ILISRTQSKL DALSADITSK YGPKIAVKTQ
     AMDFAQNKDS DYAAMKKLID GLDVSILINN VGLSHSIPVP FVETPKQEMN DIIMINCMAT
     LRVTQLVTPG MVSRNRGLVL TMASFGGFFP TPLLATYSGS KAFLQQWSTA LASELEPHGV
     YVQCVQSHLV TTAMSKIRKT SALVPNPKQF VNATLSKIGR SGGAQGVAFT STPYWSHGLM
     HWFLARFLGE RSDTVVKVNR GMHESIRKRA LKKAEREAKK Q
//
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