ID   MKAR_MALGO              Reviewed;         324 AA.
AC   A8Q1U2;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=MGL_1839;
OS   Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=425265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4612 / CBS 7966;
RX   PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA   Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA   Kronstad J.W., DeAngelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA   Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA   Chu L., Sears R., Yuan B., Dawson T.L. Jr.;
RT   "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT   virulence traits shared with plant and human fungal pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(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; AAYY01000006; EDP43626.1; -; Genomic_DNA.
DR   RefSeq; XP_001730840.1; XM_001730788.1.
DR   AlphaFoldDB; A8Q1U2; -.
DR   SMR; A8Q1U2; -.
DR   STRING; 425265.A8Q1U2; -.
DR   EnsemblFungi; EDP43626; EDP43626; MGL_1839.
DR   GeneID; 5855147; -.
DR   KEGG; mgl:MGL_1839; -.
DR   VEuPathDB; FungiDB:MGL_1839; -.
DR   InParanoid; A8Q1U2; -.
DR   OMA; FLQHWSS; -.
DR   OrthoDB; 895581at2759; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000008837; 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   PRINTS; PR00080; SDRFAMILY.
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..324
FT                   /note="Very-long-chain 3-oxoacyl-CoA reductase"
FT                   /id="PRO_0000357314"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03107"
FT   ACT_SITE        202
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03107"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03107"
SQ   SEQUENCE   324 AA;  35967 MW;  0F1C53D176C3B997 CRC64;
     MIETCLCWVG GIFIVTCIAY VVYVALEVHV FPGRSLTTYG ANPKLRGAGS WALVTGATDG
     IGREFAMQLA ARGFNIVAVS RTAEKLAILS KEIESTMPGI KTCYYAMDFL SAGNAEYEGL
     EQLIRHLDIA VLVNNVGLSH TMPVNFLEMD GRELASICQV NIVATMQVTR VVAPHLVRRG
     RGLILNLGSF SGQWSTPLLA TYAGSKAFLI AWTQALGEEM RRSHVDVQLL NTYFVVSSMS
     KVRKPSMMVP TPKNFVRSAL SRIGRSSGAL GRPFTLTPFP SHAWLDWAVE HFVPRWWLLR
     QAYDVSLDTR RRAIRKAQRL EKSQ