ID   MKAR_MAGO7              Reviewed;         331 AA.
AC   A4QTE3; G4N4E5;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=MGG_05096;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
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; CM001233; EHA52813.1; -; Genomic_DNA.
DR   RefSeq; XP_003712620.1; XM_003712572.1.
DR   AlphaFoldDB; A4QTE3; -.
DR   SMR; A4QTE3; -.
DR   STRING; 318829.MGG_05096T0; -.
DR   EnsemblFungi; MGG_05096T0; MGG_05096T0; MGG_05096.
DR   GeneID; 2675553; -.
DR   KEGG; mgr:MGG_05096; -.
DR   VEuPathDB; FungiDB:MGG_05096; -.
DR   eggNOG; KOG1014; Eukaryota.
DR   HOGENOM; CLU_010194_38_0_1; -.
DR   InParanoid; A4QTE3; -.
DR   OMA; FLQHWSS; -.
DR   OrthoDB; 895581at2759; -.
DR   UniPathway; UPA00094; -.
DR   PHI-base; PHI:8927; -.
DR   Proteomes; UP000009058; Chromosome 3.
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..331
FT                   /note="Very-long-chain 3-oxoacyl-CoA reductase"
FT                   /id="PRO_0000357313"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03107"
FT   ACT_SITE        209
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03107"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03107"
SQ   SEQUENCE   331 AA;  36134 MW;  1F3D29C71AC1C684 CRC64;
     MDSLTTALGS VPQVVQWALA GVGALYISAK VLSYLHLVLN LFILGGTNLS KYGKKGSWAV
     VTGASDGLGK EFASQLAAKG FNIVLVSRTE SKLKELAKEL EAKNGSLKTK VLAMDYEQDN
     DDDYEKLGQL LSGLDVAILI NNVGRSHSIP VPFLQTPREE LQNIVTINCL GTLKTTQVVA
     PIMAQRKRGL ILTMGSFGGW MPTPFLATYS GSKAFLQHWS TSLAEELRSS GVDVHLVLSY
     LIVSAMSKVR RPSAMVPTPR AFVRSALGKI GCATQNVAYT YTPWWSHAIM QWWVENTIGI
     GSKIGLQVNL KMHKDIRTRA LKKAEREAKK A