ID   CPXM_BACSH              Reviewed;         405 AA.
AC   P27632; E0TY13;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Cytochrome P450 109;
DE            EC=1.14.-.-;
DE   AltName: Full=ORF405;
GN   Name=cyp109; OrderedLocusNames=BSUW23_09845;
OS   Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus
OS   subtilis subsp. spizizenii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=655816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX   PubMed=1849493; DOI=10.1016/0378-1119(91)90111-n;
RA   Ahn K.S., Wake R.G.;
RT   "Variations and coding features of the sequence spanning the replication
RT   terminus of Bacillus subtilis 168 and W23 chromosomes.";
RL   Gene 98:107-112(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX   PubMed=21527469; DOI=10.1099/mic.0.048520-0;
RA   Zeigler D.R.;
RT   "The genome sequence of Bacillus subtilis subsp. spizizenii W23: insights
RT   into speciation within the B. subtilis complex and into the history of B.
RT   subtilis genetics.";
RL   Microbiology 157:2033-2041(2011).
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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; M24523; AAA22720.1; -; Genomic_DNA.
DR   EMBL; CP002183; ADM38013.1; -; Genomic_DNA.
DR   AlphaFoldDB; P27632; -.
DR   SMR; P27632; -.
DR   EnsemblBacteria; ADM38013; ADM38013; BSUW23_09845.
DR   KEGG; bss:BSUW23_09845; -.
DR   HOGENOM; CLU_033716_0_2_9; -.
DR   OMA; RDWAGMM; -.
DR   Proteomes; UP000002233; Chromosome.
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   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..405
FT                   /note="Cytochrome P450 109"
FT                   /id="PRO_0000052223"
FT   BINDING         351
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   405 AA;  45846 MW;  1331D5BEA74E3C04 CRC64;
     MTNQTARSSK KERYANLIPM EELHSEKDRL FPFPIYDKLR RESPVRYDPL RDCWDVFKYD
     DVQFVLKNPK LFSSKRGIQT ESILTMDPPK HTKLRALVSR AFTPKAVKQL ETRIKDVTAF
     LLQEARQKST IDIIEDFAGP LPVIIIAEML GAPIEDRHLI KTYSDVLVAG AKDSSDKAVA
     DMVHNRRDGH AFLSDYFRDI LSKRRAEPKE DLMTMLLQAE IDGEYLTEEQ LIGFCILLLV
     AGNETTTNLI ANAVRYLTED SVVQQQVRQN TDNVANVIEE TLRYYSPVQA IGRVATEDTE
     LGGVFIKKGS SVISWIASAN RDEDKFCKPD CFKIDRPSYP HLSFGFGIHF CLGAPLARLE
     ANIALSSLLS MSACIEKAAH DEKLEAIPSP FVFGVKRLPV RITFK