MKAR_CRYNJ
ID MKAR_CRYNJ Reviewed; 361 AA.
AC P0CR34; Q55NM3; Q5KC11;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 57.
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 OrderedLocusNames=CNI00690;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(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}.
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; AE017349; AAW45449.1; -; Genomic_DNA.
DR RefSeq; XP_572756.1; XM_572756.1.
DR AlphaFoldDB; P0CR34; -.
DR SMR; P0CR34; -.
DR STRING; 5207.AAW45449; -.
DR PaxDb; P0CR34; -.
DR EnsemblFungi; AAW45449; AAW45449; CNI00690.
DR GeneID; 3259634; -.
DR KEGG; cne:CNI00690; -.
DR VEuPathDB; FungiDB:CNI00690; -.
DR eggNOG; KOG1014; Eukaryota.
DR HOGENOM; CLU_010194_38_0_1; -.
DR InParanoid; P0CR34; -.
DR OMA; FLQHWSS; -.
DR OrthoDB; 895581at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000002149; Chromosome 9.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IBA:GO_Central.
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..361
FT /note="Very-long-chain 3-oxoacyl-CoA reductase"
FT /id="PRO_0000357307"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03107"
FT ACT_SITE 236
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03107"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03107"
SQ SEQUENCE 361 AA; 39197 MW; 4397C7DD0082B61A CRC64;
MVADTVHVGQ HLAGHPSVHL FGHEIVLDVS IPALILSTVG AAFLLRYTLS IFRLFLELTV
LPGKDIKSFQ SRKGETWAVV TGCTSGIGLE FARQLAAKKF NIILVGRRQS ALTDLSKEIE
SKYDVHTKSV TVDVSTPGSA RDDALTQLEL LAQNLDVGIL INNVGASHSM PVAFHETERS
EMSRIIETNV TWTYLVTRSI LPSMVARSKQ KGAPKSLVIT IGSLSGRIPS PLLASYSGTK
AALATWTKAL AEEVKPQGVI VELVQAAFVV SNMSKIRKSS PFVPTPAPFV RSTLNSIGLP
RGAQGRPHER TPFWSHAILD YVVGFAGYVS EMAGIKVILG MHKDIRKRAL KKAARDEKKA
E
