ID   MKAR_YEAS7              Reviewed;         347 AA.
AC   A6ZLA1;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=SCY_0371;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(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   -!- SUBUNIT: Interacts with the fatty acid elongation system components
CC       ELO3 and TSC13. {ECO:0000255|HAMAP-Rule:MF_03107}.
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}.
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; AAFW02000011; EDN64770.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZLA1; -.
DR   SMR; A6ZLA1; -.
DR   EnsemblFungi; EDN64770; EDN64770; SCY_0371.
DR   HOGENOM; CLU_010194_38_0_1; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000007060; 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   Transmembrane; Transmembrane helix.
FT   CHAIN           1..347
FT                   /note="Very-long-chain 3-oxoacyl-CoA reductase"
FT                   /id="PRO_0000357327"
FT   TRANSMEM        20..40
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;  38753 MW;  B594CFEABB2FA6FC CRC64;
     MTFMQQLQEA GERFRCINGL LWVVFGLGVL KCTTLSLRFL ALIFDLFLLP AVNFDKYGAK
     SGKYCVITGA SDGIGKEFAR QMAKRGFNLV LISRTQSKLE ALQKELEDQH HVVVKILAID
     IAEDKESNYE SIKELCAQLP ITVLVNNVGQ SHSIPVPFLE TEEKELRDII TINNTATLLI
     TQIIAPKIVE TVKAENKKSG TRGLILTMGS FGGLIPTPLL ATYSGSKSFL QSWSNSLAGE
     LSKDAIDVEL IISYLVTSSM SKIRRSSLMI PNPQQFVKST LRSVGRRCGS QERYATMTPY
     WAHAVYQFVI TETFGVYSKI VNSINYSFHK SIRIRALKKA ARQVKKE