ID CPXU_SINFN Reviewed; 447 AA.
AC P55540;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE RecName: Full=Cytochrome P450 BJ-4 homolog;
DE EC=1.14.14.-;
GN Name=cyp117A2; OrderedLocusNames=NGR_a02740; ORFNames=y4kV;
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG Plasmid sym pNGR234a.
OC Bacteria; Pseudomonadota; 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; AAB91753.1; -; Genomic_DNA.
DR PIR; T10876; T10876.
DR RefSeq; NP_443951.1; NC_000914.2.
DR RefSeq; WP_010875299.1; NC_000914.2.
DR AlphaFoldDB; P55540; -.
DR SMR; P55540; -.
DR KEGG; rhi:NGR_a02740; -.
DR PATRIC; fig|394.7.peg.292; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_001570_5_1_5; -.
DR OrthoDB; 9764248at2; -.
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 CDD; cd20614; CYPBJ-4-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR PANTHER; PTHR24286:SF24; LANOSTEROL 14-ALPHA DEMETHYLASE; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 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..447
FT /note="Cytochrome P450 BJ-4 homolog"
FT /id="PRO_0000052310"
FT BINDING 392
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 447 AA; 49855 MW; 55E4DB48438F2973 CRC64;
MNVLLNPLNR RHRLRYDIPV MPGAFPLVGH LPAIVCDLPR LLRRAERTLG SHFWLDFGPA
GHLMTCVDPH AFALLRHKDV SSALIEEIAP ELLGGTLVAQ DGGAHRQARD AIKAAFLPEG
LTQAGIGDLF APVIRARVQA WRDRGDVTIL PETGDLMLKL IFTLMGVPAQ DLPGWHRKYR
QLLQLIVAPS VDLPGLPLRR GRAARDWIDA QLRQFVRDAR AHAARTGLIN DMVSAFDRSD
DALSDDLLVA NIRLLLLAGH DTTASTMAWM VIELARQPML WDALVEEAQR VGAVPTRHAD
LEQCPVAEAL FRETLRVHPA TTLLPRRALQ ELQLGQRRIP AGTHLCIPLL HFSTSALLHE
APDQFRLARW LQRTEPIRPV DMLQFGTGPH VCIGYHLVWL ELVQFSIALA LTMHKAGVRP
LLLSGVEKGR RYYPTAHPSM TIRIGFS
//
