ID A0A1D8PHT9_CANAL Unreviewed; 526 AA.
AC A0A1D8PHT9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Acyl-CoA desaturase {ECO:0000256|PIRNR:PIRNR000345};
DE EC=1.14.19.1 {ECO:0000256|PIRNR:PIRNR000345};
GN Name=OLE2 {ECO:0000313|CGD:CAL0000198173,
GN ECO:0000313|EMBL:AOW27708.1};
GN OrderedLocusNames=CAALFM_C207090CA {ECO:0000313|EMBL:AOW27708.1},
GN orf19.9804 {ECO:0000313|CGD:CAL0000198173};
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 {ECO:0000313|EMBL:AOW27708.1, ECO:0000313|Proteomes:UP000000559};
RN [1] {ECO:0000313|EMBL:AOW27708.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
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] {ECO:0000313|EMBL:AOW27708.1, ECO:0000313|Proteomes:UP000000559}
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=17419877; DOI=.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] {ECO:0000313|EMBL:AOW27708.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=24025428; DOI=.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: Stearoyl-CoA desaturase that utilizes O(2) and electrons from
CC reduced cytochrome b5 to introduce the first double bond into saturated
CC fatty acyl-CoA substrates. {ECO:0000256|PIRNR:PIRNR000345}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA =
CC (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:19721, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57394; EC=1.14.19.1;
CC Evidence={ECO:0000256|PIRNR:PIRNR000345};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|PIRNR:PIRNR000345};
CC Note=Expected to bind 2 Fe(2+) ions per subunit.
CC {ECO:0000256|PIRNR:PIRNR000345};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000256|ARBA:ARBA00009295, ECO:0000256|PIRNR:PIRNR000345}.
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DR EMBL; CP017624; AOW27708.1; -; Genomic_DNA.
DR RefSeq; XP_714854.2; XM_709761.2.
DR AlphaFoldDB; A0A1D8PHT9; -.
DR SMR; A0A1D8PHT9; -.
DR STRING; 237561.A0A1D8PHT9; -.
DR EnsemblFungi; C2_07090C_A-T; C2_07090C_A-T-p1; C2_07090C_A.
DR GeneID; 3643503; -.
DR KEGG; cal:CAALFM_C207090CA; -.
DR CGD; CAL0000198173; OLE2.
DR VEuPathDB; FungiDB:C2_07090C_A; -.
DR eggNOG; KOG0537; Eukaryota.
DR eggNOG; KOG1600; Eukaryota.
DR InParanoid; A0A1D8PHT9; -.
DR OrthoDB; 2004328at2759; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; ISS:CGD.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IMP:CGD.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; ISS:CGD.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR InterPro; IPR009160; Acyl-CoA_deSatase_haem/ster-bd.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR005804; FA_desaturase_dom.
DR PANTHER; PTHR11351; ACYL-COA DESATURASE; 1.
DR PANTHER; PTHR11351:SF31; DESATURASE 1, ISOFORM A-RELATED; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF000345; OLE1; 2.
DR PRINTS; PR00075; FACDDSATRASE.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|PIRNR:PIRNR000345};
KW Fatty acid biosynthesis {ECO:0000256|PIRNR:PIRNR000345};
KW Fatty acid metabolism {ECO:0000256|PIRNR:PIRNR000345};
KW Heme {ECO:0000256|PIRNR:PIRNR000345}; Iron {ECO:0000256|PIRNR:PIRNR000345};
KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000345};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000345};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR000345};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000345};
KW Reference proteome {ECO:0000313|Proteomes:UP000000559};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|PIRNR:PIRNR000345}.
FT TRANSMEM 61..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 409..491
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 505..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 526 AA; 60862 MW; D6C7C11CC5EAADBE CRC64;
MSKHSEDPIK GVKVQKRKVA SIASTSSSTS THQQLMNQAT KMKRTKINEM KKQKQDFFKR
INYSHLLTVV VLPLLAVLYV VLCKQSIVPE NERTLYFTCI YYNITMLAFT SGYHKYFAHN
SFKVKAELLK YYFCIFGSSC GLGSVRWWAG LHRAHHHFTD DTERDPYSIK RGFLFSHYAW
LLKKPKLTKF YLDFLEQEFP EHAENQKVQN EIVLDKEIET EYNGEDIMRQ NYDESLRNLL
MWQQRTYLFW FFVTTILIPA LITKYVCGDS IVHGILYPGI LRMFLCQQSL LSTESICHLK
RIQVTIPTQP FNDKNSSTNC NNPLVSFLTY GQSHQNYHHE FPHDYRVDNS YLTYDPTKWF
IWILEQLGAV DELSRTPGNL IVQLKLQQQQ LIINRTKSQL NWGTPISKLP LISPSDFKKI
ISSTSNKDRI YIVIQNIIHD ITPFMDQHPG GVALLKASHG KDATKAFYGG VYGHSTAAVN
LLATMRIGVL DDGDDEEVWR RVAREEREVS NSTDSRPGHH HTAEAA
//
