GenomeNet

Database: UniProt
Entry: P14762
LinkDB: P14762
Original site: P14762 
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   29-OCT-2014, entry version 77.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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-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; -; 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; SSF48264; 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
//
DBGET integrated database retrieval system