MKAR_VANPO
ID MKAR_VANPO Reviewed; 347 AA.
AC A7TMJ2;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Very-long-chain 3-oxoacyl-CoA reductase {ECO:0000255|HAMAP-Rule:MF_03107};
DE EC=1.1.1.330 {ECO:0000255|HAMAP-Rule:MF_03107};
DE AltName: Full=3-ketoacyl-CoA reductase {ECO:0000255|HAMAP-Rule:MF_03107};
DE Short=3-ketoreductase {ECO:0000255|HAMAP-Rule:MF_03107};
DE Short=KAR {ECO:0000255|HAMAP-Rule:MF_03107};
DE AltName: Full=Microsomal beta-keto-reductase {ECO:0000255|HAMAP-Rule:MF_03107};
GN ORFNames=Kpol_513p6;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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:0000255|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:0000255|HAMAP-Rule:MF_03107};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:P38286}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03107}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03107}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000255|HAMAP-Rule:MF_03107}.
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DR EMBL; DS480423; EDO16490.1; -; Genomic_DNA.
DR RefSeq; XP_001644348.1; XM_001644298.1.
DR AlphaFoldDB; A7TMJ2; -.
DR SMR; A7TMJ2; -.
DR STRING; 436907.A7TMJ2; -.
DR EnsemblFungi; EDO16490; EDO16490; Kpol_513p6.
DR GeneID; 5544659; -.
DR KEGG; vpo:Kpol_513p6; -.
DR eggNOG; KOG1014; Eukaryota.
DR HOGENOM; CLU_010194_38_0_1; -.
DR InParanoid; A7TMJ2; -.
DR OMA; FLQHWSS; -.
DR OrthoDB; 895581at2759; -.
DR PhylomeDB; A7TMJ2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102339; F:3-oxo-arachidoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102340; F:3-oxo-behenoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102342; F:3-oxo-cerotoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102341; F:3-oxo-lignoceroyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0045703; F:ketoreductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030497; P:fatty acid elongation; IEA:UniProtKB-UniRule.
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 Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..347
FT /note="Very-long-chain 3-oxoacyl-CoA reductase"
FT /id="PRO_0000357324"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03107"
FT ACT_SITE 223
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03107"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03107"
SQ SEQUENCE 347 AA; 38665 MW; 50FF59A1C66F333D CRC64;
MLDSFMTQLE IVGNRSKCVN MLLWSIFGFG VLKATTLILR IMACFVDLFV LPPVNYSKYG
SKNGNYCVIT GASDGIGKEF AFQMAKRGFN LILISRTLSK LETLQKEIST KYNVKVEVLA
IDVAKDSEDN YSAIKELCGK FPITALINNV GQSHSIPVPF LETDEDEMRR IITINNTATL
MITQIIAPMI IKTTKESSKK TRGLILTMGS FGGLIPTPLL ATYSGSKAFL QSWSSSLAGE
LKEHNVDVEL IISYLVTSSM SKIRKTSMMI PNPKTFVAST LRNIGRRCGA QERYATITPY
WSHALYQLAI VEAVGVYSHL VNYINYVFHK SIRIRALKKA ARDAKKQ
