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}.
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; 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
//