ID   CPXG_STRSQ              Reviewed;         381 AA.
AC   P23296;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Cytochrome P450 105C1;
DE            EC=1.14.-.-;
GN   Name=cyp105C1; Synonyms=choP;
OS   Streptomyces sp.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2361941; DOI=10.1128/jb.172.7.3644-3653.1990;
RA   Horii M., Ishizaki T., Paik S.Y., Manome T., Murooka Y.;
RT   "An operon containing the genes for cholesterol oxidase and a cytochrome P-
RT   450-like protein from a Streptomyces sp.";
RL   J. Bacteriol. 172:3644-3653(1990).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; M31939; AAA26718.1; -; Genomic_DNA.
DR   PIR; S15809; S15809.
DR   AlphaFoldDB; P23296; -.
DR   SMR; P23296; -.
DR   PRIDE; P23296; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..381
FT                   /note="Cytochrome P450 105C1"
FT                   /id="PRO_0000052216"
FT   BINDING         330
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:0000250"
SQ   SEQUENCE   381 AA;  41704 MW;  841B959C9DDEA99C CRC64;
     MTQAAPVTFS TVRENYFGPP AEMQALRHKA PVTRTAFADG RPGWLVTGYS AARAVLSDSR
     FTARGEREHP AVPRAATLED ERCRRLIAGQ FTARRMRQLT GRTERIVREH LDAMEHMGSP
     ADLVEHFALP VPSLVIAELL GVPPPDREHF QHDTLRWGGF GRSTEEVTEA FVSLGGQLQR
     LVRLKRTEPG DDLLSGLIAA DPALTDEELA SIAFLLLVAG HGTTAHQIAL GAFLLLEHPD
     QLAALRADPA LTESAVEELL RHLSVVHHGP TRAALQDADI EGTPVKAGEV VVVSLGAANR
     DPARFERPDA VDVTREDTGH LAFGHGMHQC LGRQLARIEL RVALTALLER FPHLRLACPA
     AEIPLRHDMQ VYGADRLPVA W