ID   CPXP_SINFN              Reviewed;         400 AA.
AC   P55544;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Cytochrome P450 BJ-1 homolog;
DE            EC=1.14.14.-;
GN   Name=cyp112A2; OrderedLocusNames=NGR_a02700; ORFNames=y4lD;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234a.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=9163424; DOI=10.1038/387394a0;
RA   Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA   Perret X.;
RT   "Molecular basis of symbiosis between Rhizobium and legumes.";
RL   Nature 387:394-401(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; U00090; AAB91757.1; -; Genomic_DNA.
DR   RefSeq; NP_443955.1; NC_000914.2.
DR   RefSeq; WP_010875295.1; NC_000914.2.
DR   AlphaFoldDB; P55544; -.
DR   SMR; P55544; -.
DR   STRING; 394.NGR_a02700; -.
DR   EnsemblBacteria; AAB91757; AAB91757; NGR_a02700.
DR   KEGG; rhi:NGR_a02700; -.
DR   PATRIC; fig|394.7.peg.288; -.
DR   eggNOG; COG2124; Bacteria.
DR   HOGENOM; CLU_033716_1_1_5; -.
DR   OMA; RDWAGMM; -.
DR   OrthoDB; 816674at2; -.
DR   Proteomes; UP000001054; Plasmid sym pNGR234a.
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; Plasmid;
KW   Reference proteome.
FT   CHAIN           1..400
FT                   /note="Cytochrome P450 BJ-1 homolog"
FT                   /id="PRO_0000052308"
FT   BINDING         349
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   400 AA;  44248 MW;  FB34E493E54965EA CRC64;
     MPEQPLPTLP MWRVDHIEPS PTMLALRANG PIHNVRFPRG HEGWWVTGYD EAKAVLSDAA
     FRPAGMPPAA FTPDCVILGS PGWLVSHEGG EHARLRTIVA PAFSDRRVKL LAQQVEAIAA
     QLFETLAAQP QPADLRRHLS FPLPAMVISA LMGVLYEDHA FFAGLSDEVM THQHESGPRS
     ASRLAWEELR AYIRGKMRDK RQDPGDNLLT DLLAAVDRGE ATEEEAIGLA AGMLVAGHES
     TVAQIEFGLL AMLRHPQQRE RLVGNPSLVD KAVEEILRMY PPGAGWDGIM RYPRTDVTIA
     GVHIPAESKV LVGLPATSFD PRHFEDPEIF DIGRDAKPHL AFSYGPHYCI GMALARLELK
     VVFGSIFQRF PALRLAVAPE ELKLRKEIIT GGFEEFPVLW