ID A0A094ATS6_9PEZI Unreviewed; 333 AA.
AC A0A094ATS6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=V493_01704 {ECO:0000313|EMBL:KFY30758.1};
OS Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY30758.1, ECO:0000313|Proteomes:UP000029327};
RN [1] {ECO:0000313|EMBL:KFY30758.1, ECO:0000313|Proteomes:UP000029327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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|HAMAP-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:KFY30758.1}.
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DR EMBL; JPJV01000625; KFY30758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094ATS6; -.
DR STRING; 1420906.A0A094ATS6; -.
DR HOGENOM; CLU_010194_38_0_1; -.
DR OrthoDB; 6845at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000029327; 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}; Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03107};
KW Lipid metabolism {ECO:0000256|HAMAP-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:UP000029327};
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 ACT_SITE 208
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03107"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03107"
SQ SEQUENCE 333 AA; 36013 MW; 94EABE9288B918D4 CRC64;
MAINDILAAV PKPVTVGFAA LGALWLGRKV VSYIALLLDL FILSGTNLRK YGPKGTWAVI
TGASDGLGKE YAVQLASKGF NILLVSRTES KLATLAREIE NKTPAIKTKY LAMDFSKDNA
ADYAKLKAMV DDLDVGILIN NVGQSHSYPV PFLLTPHKEM RDIITINCLG TLEVTRLVAP
GMAQRKRGLI LTMGSFGGLL PTPLLATYSG SKAFLQNWST SLASELAPQG VDVQLVLSYL
VASAMSKIRR PSATIPNPRN FVKSVLGSIG LSGGARKTAN TSTPFWTHAL MQWWIENTTG
TSSPTTVAIN KKLHQDIRTR ALKKIERDSK KST
//