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Database: UniProt
Entry: C0NSR3_AJECG
LinkDB: C0NSR3_AJECG
Original site: C0NSR3_AJECG 
ID   C0NSR3_AJECG            Unreviewed;       533 AA.
AC   C0NSR3;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=sterol 22-desaturase {ECO:0000256|ARBA:ARBA00039038};
DE            EC=1.14.19.41 {ECO:0000256|ARBA:ARBA00039038};
GN   ORFNames=HCBG_06193 {ECO:0000313|EMBL:EEH05929.1};
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH05929.1, ECO:0000313|Proteomes:UP000001631};
RN   [1] {ECO:0000313|Proteomes:UP000001631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC   {ECO:0000313|Proteomes:UP000001631};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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; GG663370; EEH05929.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0NSR3; -.
DR   STRING; 447093.C0NSR3; -.
DR   VEuPathDB; FungiDB:I7I50_06564; -.
DR   HOGENOM; CLU_023517_0_0_1; -.
DR   InParanoid; C0NSR3; -.
DR   OrthoDB; 5393233at2759; -.
DR   Proteomes; UP000001631; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF228; C-22 STEROL DESATURASE ERG5; 1.
DR   PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
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|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602403-1};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001631};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         478
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   533 AA;  60947 MW;  252614F71DFAE6CD CRC64;
     MDTLNGSFAS PVADVGLASS VARDPAGLLM SIYNGMTLWT TIFTILLLLV TYDQVKYIWL
     KGSIEGPRFK IPFMGPFLQS VNPKFPEYQA KWASGELSCV SVFHKFVVIA ATRDMSRKVF
     NSPSYVKPCV VDVAHKLLGK DNWVFLDGKE HVEFRKGLNG LFTRAALTNY MPQLEDVYDR
     FYNMFVQRSE ELNMKPEPWM PHFRELMTAL SCRTFVGHYM SDEAVKHVAD DYYLITAALE
     LVNFPIIIPF TKTWYGKRSS DMVLREFTKC AAKSKVRMAN GEKVTCIMDA WVKNMLDSAA
     YREKIAKGLP VEDSEKPAHI LRDFTDYEIA QTIFTFLFAS QDATSSASTW LFQLLSDRPE
     ILAKVREENL RIRGGDRNVP ISMELLDQMD YTRAVVRETL RYRPPVIMVP YMVKKDFPVT
     DTYTLPKGSM IIPSVWPSTH DPEAYPDPET FNPERWLNGE ADKAAKNFLV FGTGPHYCLG
     QTYAQLNLMA MIGKASMLLD WEHHTTPTSE DIRVFATIFP EDDCPLVFRR RPE
//
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