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Database: UniProt
Entry: B9WKF0_CANDC
LinkDB: B9WKF0_CANDC
Original site: B9WKF0_CANDC 
ID   B9WKF0_CANDC            Unreviewed;       517 AA.
AC   B9WKF0;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   RecName: Full=sterol 22-desaturase {ECO:0000256|ARBA:ARBA00039038};
DE            EC=1.14.19.41 {ECO:0000256|ARBA:ARBA00039038};
GN   OrderedLocusNames=Cd36_72510 {ECO:0000313|CGD:CAL0000160930};
GN   ORFNames=CD36_72510 {ECO:0000313|EMBL:CAX40802.1};
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX40802.1, ECO:0000313|Proteomes:UP000002605};
RN   [1] {ECO:0000313|EMBL:CAX40802.1, ECO:0000313|Proteomes:UP000002605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC   {ECO:0000313|Proteomes:UP000002605};
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(2009).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR602403-1};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; FM992694; CAX40802.1; -; Genomic_DNA.
DR   RefSeq; XP_002421465.1; XM_002421420.1.
DR   AlphaFoldDB; B9WKF0; -.
DR   GeneID; 8049015; -.
DR   KEGG; cdu:CD36_72510; -.
DR   CGD; CAL0000160930; Cd36_72510.
DR   VEuPathDB; FungiDB:CD36_72510; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_023517_0_0_1; -.
DR   OrthoDB; 5393233at2759; -.
DR   Proteomes; UP000002605; Chromosome 7.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd11082; CYP61_CYP710; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR   PANTHER; PTHR24286:SF228; CYTOCHROME P450 61; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022955};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR602403-1,
KW   ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955};
KW   Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW   Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011};
KW   Sterol metabolism {ECO:0000256|ARBA:ARBA00023166}.
FT   BINDING         458
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602403-1"
SQ   SEQUENCE   517 AA;  59530 MW;  23220251FD2A7600 CRC64;
     MNSTEVDNLP LHEQLTSFVE LAIAKATGSP ITTLFTIIFL ILSYDQLSYQ INKGSIAGPR
     FKFYPIIGPF LESLDPKFEE YKAKWDSGEL SCVSIFHKFV VIASSRDLAR KILSSPKYVK
     PCVVDVAVKI LRPSNWVFLD GKQHTDYRRS LNGLFSSKAL EIYIPVQEKY MDIYLEKFCN
     YDGPREFFPE FRELLCALSL RTFCGDYITD DQIAVVADNY YRVTAALELV NFPIIIPYTK
     TWYGKKIADD SMKVFENCAA MAKKHINENN GTPTCVMDEW IHLMKEAREK HSEDPDSKLL
     VREFSNREIS EVIFTFLFAS QDASSSLACW LFQIVADRPD VVAKIREEQL RVRNNNPDLR
     LSLDLINQMT YTNNVVKETL RYRPPVLMVP YVVKKSFPVT ESYTAPKGAM IIPTLYPALH
     DPEVYDEPDS FIPERWENAS GDMYKRNWLV FGTGPHVCLG KNYVLMLFTG MLGKFVMNSD
     MIHHKTDLSE EIKVFATIFP KDDLILEWKK RDPLKSL
//
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