ID A0A1Y2FQ79_9BASI Unreviewed; 340 AA.
AC A0A1Y2FQ79;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Very-long-chain 3-oxoacyl-CoA reductase {ECO:0000256|HAMAP-Rule:MF_03107};
DE EC=1.1.1.330 {ECO:0000256|HAMAP-Rule:MF_03107};
DE AltName: Full=3-ketoacyl-CoA reductase {ECO:0000256|HAMAP-Rule:MF_03107};
DE Short=3-ketoreductase {ECO:0000256|HAMAP-Rule:MF_03107};
DE Short=KAR {ECO:0000256|HAMAP-Rule:MF_03107};
DE AltName: Full=Microsomal beta-keto-reductase {ECO:0000256|HAMAP-Rule:MF_03107};
GN ORFNames=BCR35DRAFT_302841 {ECO:0000313|EMBL:ORY85366.1};
OS Leucosporidium creatinivorum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Leucosporidiales; Leucosporidium.
OX NCBI_TaxID=106004 {ECO:0000313|EMBL:ORY85366.1, ECO:0000313|Proteomes:UP000193467};
RN [1] {ECO:0000313|EMBL:ORY85366.1, ECO:0000313|Proteomes:UP000193467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=62-1032 {ECO:0000313|EMBL:ORY85366.1,
RC ECO:0000313|Proteomes:UP000193467};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_03107};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03107}; Single-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_03107}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|HAMAP-Rule:MF_03107}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORY85366.1}.
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DR EMBL; MCGR01000016; ORY85366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2FQ79; -.
DR STRING; 106004.A0A1Y2FQ79; -.
DR InParanoid; A0A1Y2FQ79; -.
DR OrthoDB; 6845at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000193467; 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 SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP-
KW Rule:MF_03107};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW Rule:MF_03107};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_03107}; Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03107};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03107};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03107};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_03107};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03107}; Reference proteome {ECO:0000313|Proteomes:UP000193467};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03107};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_03107}.
FT TRANSMEM 20..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03107"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03107"
SQ SEQUENCE 340 AA; 36759 MW; A05B5B98BD77DBDB CRC64;
MSDFAVLKAR AAALTGECPW TTLALALVGA GWLSTYVLSF ARMLVDLARP GIPLKKFGAK
KGAWAVVTGA TAGIGRDFAL QLAGAGFNVF LASRTASKLQ EISDEITAKY PQAKTQVHSI
DFAAATADDY KALGVALSPL DIGILINNVG KSYDEPTFYQ DLSDQDIADI VEINVNATLK
VTKLVVPGMI ARKRGLILSV GSFAALIPSP LLAVYSGSKA FLSSWSQALG SELEGTGVHV
ELLNAYFITS KLSKIRKSSW MIPTPATYVR SVLAHIGVNG GAVGQPHIST PYHGHAPVQW
VVDHLFTRSW WLSYNRKLHV DIRRRAIRKR ERLAKEAKSQ
//
