ID   CPXF_STRGO              Reviewed;         403 AA.
AC   P18327;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Cytochrome P450-SU2;
DE            EC=1.14.-.-;
DE   AltName: Full=CYP105B1;
DE   AltName: Full=Cytochrome P450-CVB1;
GN   Name=cyp105B1; Synonyms=subC;
OS   Streptomyces griseolus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-33.
RC   STRAIN=ATCC 11796 / DSM 40854;
RX   PubMed=2345149; DOI=10.1128/jb.172.6.3335-3345.1990;
RA   Omer C.A., Lenstra R., Litle P.J., Dean C., Tepperman J.M., Leto K.J.,
RA   Romesser J.A., O'Keefe D.P.;
RT   "Genes for two herbicide-inducible cytochromes P-450 from Streptomyces
RT   griseolus.";
RL   J. Bacteriol. 172:3335-3345(1990).
CC   -!- FUNCTION: Metabolism of a number of sulfonylurea herbicides.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- INDUCTION: By herbicides.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; M32239; AAA26825.1; -; Genomic_DNA.
DR   PIR; B35401; B35401.
DR   AlphaFoldDB; P18327; -.
DR   SMR; P18327; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Iron; Metal-binding; Monooxygenase;
KW   Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2345149"
FT   CHAIN           2..403
FT                   /note="Cytochrome P450-SU2"
FT                   /id="PRO_0000052215"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         352
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   403 AA;  44410 MW;  F8494705DDFEDEB5 CRC64;
     MTTAERTAPP DALTVPASRA PGCPFDPAPD VTEAARTEPV TRATLWDGSS CWLVTRHQDV
     RAVLGDPRFS ADAHRTGFPF LTAGGREIIG TNPTFLRMDD PEHARLRRML TADFIVKKVE
     AMRPEVQRLA DDLVDRMTTG RTSADLVTEF ALPLPSLVIC LLLGVPYEDH AFFQERSRVL
     LTLRSTPEEV RAAQDELLEY LARLARTKRE RPDDAIISRL VARGELDDTQ IATMGRLLLV
     AGHETTANMT ALSTLVLLRN PDQLARLRAE PALVKGAVEE LLRYLTIVHN GVPRIATEDV
     LIGGRTIAAG EGVLCMISSA NRDAEVFPGG DDLDVARDAR RHVAFGFGVH QCLGQPLARV
     ELQIAIETLL RRLPDLRLAV PHEEIPFRGD MAIYGVHSLP IAW