ID   O87605_9ACTO            Unreviewed;       416 AA.
AC   O87605;
DT   01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1998, sequence version 1.
DT   19-JAN-2010, entry version 49.
DE   SubName: Full=Cytochrome P450 hydroxylase PiKC;
DE   SubName: Full=Cytochrome P450 monooxygenase;
GN   Name=picK; Synonyms=pikC;
OS   Streptomyces venezuelae.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=54571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC15439;
RX   MEDLINE=98453342; PubMed=9778370; DOI=10.1021/bi981699c;
RA   Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.;
RT   "Characterization of the macrolide P-450 hydroxylase from Streptomyces
RT   venezuelae which converts narbomycin to picromycin.";
RL   Biochemistry 37:14937-14942(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC15439;
RX   MEDLINE=98445333; PubMed=9770448; DOI=10.1073/pnas.95.21.12111;
RA   Xue Y., Zhao L., Liu H.W., Sherman D.H.;
RT   "A gene cluster for macrolide antibiotic biosynthesis in Streptomyces
RT   venezuelae: architecture of metabolic diversity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:12111-12116(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC15439;
RX   MEDLINE=99051447; PubMed=9831532; DOI=10.1016/S1074-5521(98)90293-9;
RA   Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.;
RT   "Hydroxylation of macrolactones YC-17 and narbomycin is mediated by
RT   the pikC-encoded cytochrome P450 in Streptomyces venezuelae.";
RL   Chem. Biol. 5:661-667(1998).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; AF087022; AAC64105.1; -; Genomic_DNA.
DR   EMBL; AF079139; AAC68886.1; -; Genomic_DNA.
DR   PDB; 2BVJ; X-ray; 2.10 A; A/B=1-416.
DR   PDB; 2C6H; X-ray; 2.35 A; A/B=1-416.
DR   PDB; 2C7X; X-ray; 1.75 A; A=1-416.
DR   PDB; 2CA0; X-ray; 2.85 A; A/B=1-416.
DR   PDB; 2CD8; X-ray; 1.70 A; A/B=1-416.
DR   PDB; 2VZ7; X-ray; 3.20 A; A/B=1-416.
DR   PDB; 2VZM; X-ray; 1.85 A; A/B=1-416.
DR   PDB; 2WHW; X-ray; 2.20 A; A/B=1-416.
DR   PDB; 2WI9; X-ray; 2.00 A; A/B=1-416.
DR   PDBsum; 2BVJ; -.
DR   PDBsum; 2C6H; -.
DR   PDBsum; 2C7X; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017973; Cyt_P450_C.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
SQ   SEQUENCE   416 AA;  46038 MW;  B7392C742045F06B CRC64;
     MRRTQQGTTA SPPVLDLGAL GQDFAADPYP TYARLRAEGP AHRVRTPEGD EVWLVVGYDR
     ARAVLADPRF SKDWRNSTTP LTEAEAALNH NMLESDPPRH TRLRKLVARE FTMRRVELLR
     PRVQEIVDGL VDAMLAAPDG RADLMESLAW PLPITVISEL LGVPEPDRAA FRVWTDAFVF
     PDDPAQAQTA MAEMSGYLSR LIDSKRGQDG EDLLSALVRT SDEDGSRLTS EELLGMAHIL
     LVAGHETTVN LIANGMYALL SHPDQLAALR ADMTLLDGAV EEMLRYEGPV ESATYRFPVE
     PVDLDGTVIP AGDTVLVVLA DAHRTPERFP DPHRFDIRRD TAGHLAFGHG IHFCIGAPLA
     RLEARIAVRA LLERCPDLAL DVSPGELVWY PNPMIRGLKA LPIRWRRGRE AGRRTG
//