ID CPXI_PRIM2 Reviewed; 410 AA. AC P14762; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 03-MAY-2023, entry version 100. DE RecName: Full=Cytochrome P450(BM-1); DE EC=1.14.14.-; GN Name=cyp106; OS Priestia megaterium (strain ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / OS NBRC 15308 / NCIMB 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19) OS (Bacillus megaterium). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia. OX NCBI_TaxID=1348623; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-25. RC STRAIN=ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB RC 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19; 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 sequence RT 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. RC STRAIN=ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB RC 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19; 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 proteins, RT putative positive transcription factors involved in barbiturate-mediated RT induction of the genes encoding cytochrome P450BM-1 of Bacillus RT megaterium."; RL J. Biol. Chem. 270:18615-18625(1995). CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. CC They oxidize a variety of structurally unrelated compounds, including CC steroids, fatty acids, and xenobiotics. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X16610; CAA34612.1; -; Genomic_DNA. DR EMBL; S79230; AAC60495.1; -; mRNA. DR PIR; S07764; O4BS6M. DR RefSeq; WP_034652854.1; NZ_JJMH01000025.1. DR AlphaFoldDB; P14762; -. DR SMR; P14762; -. 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 CDD; cd11032; P450_EryK-like; 1. DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR46696; P450, PUTATIVE (EUROFUNG)-RELATED; 1. DR PANTHER; PTHR46696:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1. 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 FT /note="Cytochrome P450(BM-1)" FT /id="PRO_0000052218" FT BINDING 356 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" 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 //