CPXR_SINFN
ID CPXR_SINFN Reviewed; 467 AA.
AC P55543;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cytochrome P450 BJ-3 homolog;
DE EC=1.14.14.-;
GN OrderedLocusNames=NGR_a02710; ORFNames=y4lC;
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; AAB91756.1; -; Genomic_DNA.
DR PIR; T10879; T10879.
DR RefSeq; NP_443954.1; NC_000914.2.
DR RefSeq; WP_010875296.1; NC_000914.2.
DR AlphaFoldDB; P55543; -.
DR SMR; P55543; -.
DR STRING; 394.NGR_a02710; -.
DR EnsemblBacteria; AAB91756; AAB91756; NGR_a02710.
DR KEGG; rhi:NGR_a02710; -.
DR PATRIC; fig|394.7.peg.289; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_033716_1_0_5; -.
DR OMA; CDFARDV; -.
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..467
FT /note="Cytochrome P450 BJ-3 homolog"
FT /id="PRO_0000052309"
FT REGION 444..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 376
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 467 AA; 50695 MW; 42BC64A0E939490D CRC64;
MDMQETTTAC ADAFAELASP ACIDDPYPFM RWLREHDPVH RAASGLFLLS RHADICWALK
ATGDAFRGPA PGELARYFPR AATSLSLNLL ASTLAMKEPP THTRLRRLIS RDFTMREIDN
LRPSIARFVA ARLDGMAPAL ERGEAVDLHR QFALALPMLV FAELFGMPQD DMFGLAAGIG
AILEGLSPHA SDPQLAAADA ASARMKAYFG DLIQRKCIDP RHDIVATLVG AHDDDADTLS
DAELISMLWG MLLGGFATTA ATIDHAVLAM LAYPDQRHWL QGDAAGVEAF VEEVLRCDAP
AMFSSIPRIA QSDIELSGVV IPKNADVRVL IAAGNRDPDA FADPDRFDPA RFYGTSPGMS
TDGKIMLSFG HGIHFCLGAQ LARVQLAESL PRIQARFPTL TVAEQPTREP SAFLRTFRAL
PVRLHAQGDS PRLTSAFLNG QRGVEGGASF EHGDGERRSA TDRRAQP