ID CPXI_BACME Reviewed; 410 AA.
AC P14762;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-APR-2013, entry version 73.
DE RecName: Full=Cytochrome P450(BM-1);
DE EC=1.14.14.-;
GN Name=cyp106;
OS Bacillus megaterium.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1404;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-25.
RC STRAIN=ATCC 14581 / DSM 32 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC
RC 10342 / VKM B-512;
RX PubMed=2597681; DOI=10.1016/0167-4781(89)90120-6;
RA He J.S., Ruettinger R.T., Liu H.-M., Fulco A.J.;
RT "Molecular cloning, coding nucleotides and the deduced amino acid
RT sequence of P-450BM-1 from Bacillus megaterium.";
RL Biochim. Biophys. Acta 1009:301-303(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
RX PubMed=7629192; DOI=10.1074/jbc.270.31.18615;
RA He J.S., Liang Q., Fulco A.J.;
RT "The molecular cloning and characterization of BM1P1 and BM1P2
RT proteins, putative positive transcription factors involved in
RT barbiturate-mediated induction of the genes encoding cytochrome
RT P450BM-1 of Bacillus megaterium.";
RL J. Biol. Chem. 270:18615-18625(1995).
CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate
CC monooxygenases. They oxidize a variety of structurally unrelated
CC compounds, including steroids, fatty acids, and xenobiotics.
CC -!- COFACTOR: Heme group (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR EMBL; X16610; CAA34612.1; -; Genomic_DNA.
DR EMBL; S79230; AAC60495.1; -; mRNA.
DR PIR; S07764; O4BS6M.
DR ProteinModelPortal; P14762; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
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 Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
DR SUPFAM; SSF48264; Cytochrome_P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Monooxygenase; Oxidoreductase.
FT CHAIN 1 410 Cytochrome P450(BM-1).
FT /FTId=PRO_0000052218.
FT METAL 356 356 Iron (heme axial ligand).
SQ SEQUENCE 410 AA; 47461 MW; C9AE293E76745387 CRC64;
MNKEVIPVTE IPKFQSRAEE FFPIQWYKEM LNNSPVYFHE ETNTWNVFQY EHVKQVLSNY
DFFSSDGQRT TIFVGDNSKK KSTSPITNLT NLDPPDHRKA RSLLAAAFTP RSLKNWEPRI
KQIAADLVEA IQKNSTINIV DDLSSPFPSL VIADLFGVPV KDRYQFKKWV DILFQPYDQE
RLEEIEQEKQ RAGAEYFQYL YPIVIEKRSN LSDDIISDLI QAEVDGETFT DEEIVHATML
LLGAGVETTS HAIANMFYSF LYDDKSLYSE LRNNRELAPK AVEEMLRYRF HISRRDRTVK
QDNELLGVKL KKGDVVIAWM SACNMDETMF ENPFSVDIHR PTNKKHLTFG NGPHFCLGAP
LARLEMKIIL EAFLEAFSHI EPFEDFELEP HLTASATGQS LTYLPMTVYR
//
