MKAR_CANAL
ID MKAR_CANAL Reviewed; 349 AA.
AC Q59V93; A0A1D8PT52;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 3.
DT 03-AUG-2022, entry version 110.
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=CAALFM_CR06070WA; ORFNames=CaO19.11340, CaO19.3859;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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 -!- SEQUENCE CAUTION:
CC Sequence=AOW31318.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP017630; AOW31318.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_713488.2; XM_708395.2.
DR AlphaFoldDB; Q59V93; -.
DR SMR; Q59V93; -.
DR STRING; 237561.Q59V93; -.
DR GeneID; 3644840; -.
DR KEGG; cal:CAALFM_CR06070WA; -.
DR CGD; CAL0000189692; orf19.11340.
DR eggNOG; KOG1014; Eukaryota.
DR HOGENOM; CLU_010194_38_0_1; -.
DR InParanoid; Q59V93; -.
DR OrthoDB; 895581at2759; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q59V93; -.
DR Proteomes; UP000000559; Chromosome R.
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 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..349
FT /note="Very-long-chain 3-oxoacyl-CoA reductase"
FT /id="PRO_0000357302"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03107"
FT ACT_SITE 221
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03107"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03107"
SQ SEQUENCE 349 AA; 38359 MW; 368E7878C35E9ACC CRC64;
MPFTQFLDKY SDNLAIQYAI IFALLLGVFK LTVFSLKFAS LIYDIFLAPA TDFSKYGAAS
GKWAVVTGAS DGIGKEYAFQ LAKKGFSIVL VSRTQSKLEL IATEIESKYK VNTKIVAFDA
STDDEENYLK LEKAVFDLPV TILINNVGQS HSIPVPFLKT EKKELKDIIT INTTATLRIT
QIVAPIIVST VENPHPKQLR GLILTMGSFG GLLPTPYLAT YSGSKSFLQA WSAALAGELQ
ADHVDVELVI SYLVASAMSK IKRTSLSIPN PKQFVTSTLN GVGRRNGAQE RFATSTPYWT
HALMHFAIDN TVGVYSKIAN KLNLQMHQSI RRRALKKAAR LAAAAEKKD
