ID C6H8G8_AJECH Unreviewed; 461 AA.
AC C6H8G8;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Bifunctional P-450:NADPH-P450 reductase {ECO:0000313|EMBL:EER42601.1};
GN ORFNames=HCDG_02499 {ECO:0000313|EMBL:EER42601.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER42601.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
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.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|RuleBase:RU000461}.
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DR EMBL; GG692421; EER42601.1; -; Genomic_DNA.
DR AlphaFoldDB; C6H8G8; -.
DR STRING; 544712.C6H8G8; -.
DR VEuPathDB; FungiDB:HCDG_02499; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_5_4_1; -.
DR OMA; VAPGFNI; -.
DR Proteomes; UP000002624; 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 Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF108; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000002624};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 258..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 461 AA; 50827 MW; 993CEA3F73844656 CRC64;
MTTPIPGPPG VPLLGNIFDI NPKDTWGTSS QQCVSANSPA GEIYKVNALG HQIVFIGSAA
LLEEICDETR FRKCVTGPVV EIRRAVHDSL FTAYHHEKSW DVAHRIMAPL VSPSAAEAMF
TQMVECAATL VSRWTSDPGQ RIDVTSDLQR SDLQSVLACY FNQSANYFGG PEPSMIAAMQ
NSTLEAMKRP NRPKLLTRLL YQRKFDKDIK TMRSFAAEII ANRKSESTPK SDMLNALLNN
PDPETGEVLG EERVIDEIIT IFIGSATAPC LVSFAVYYLL QNPEEIVKAR DEIDSILGAN
GEITSSNLSS FAYCEAILRE AFRLSAVAPA FNIEPIPSDE PGEVQLAGGK YQISRKQPMI
AVLSAVNRDP AVFDEPEAFK PERMLGEAYD KLPSGVKKGF GNGKRRCFGK VPAWQWCLIT
LISILRKVDL TLAKKDYKLA SNGAFCVRPL EFFALAGPRE R
//