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 08-NOV-2023, entry version 78.
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 GeneID; 5855147; -.
DR KEGG; mgl:MGL_1839; -.
DR VEuPathDB; FungiDB:MGL_1839; -.
DR InParanoid; A8Q1U2; -.
DR OMA; LVAPGMM; -.
DR OrthoDB; 6845at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000008837; 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 PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 donor"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT ACT_SITE 206
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 53
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:L0E2Z4"
FT BINDING 108
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:L0E2Z4"
FT BINDING 116
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:L0E2Z4"
FT BINDING 135
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 170
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:L0E2Z4"
FT BINDING 202
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 206
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 235
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 237
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:L0E2Z4"
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
//