ID B5ZVA1_RHILW Unreviewed; 466 AA.
AC B5ZVA1;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:ACI57247.1};
GN OrderedLocusNames=Rleg2_3985 {ECO:0000313|EMBL:ACI57247.1};
OS Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395492 {ECO:0000313|EMBL:ACI57247.1, ECO:0000313|Proteomes:UP000008330};
RN [1] {ECO:0000313|EMBL:ACI57247.1, ECO:0000313|Proteomes:UP000008330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM2304 {ECO:0000313|EMBL:ACI57247.1,
RC ECO:0000313|Proteomes:UP000008330};
RX PubMed=21304679; DOI=10.4056/sigs.44642;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT WSM2304, an effective microsymbiont of the South American clover Trifolium
RT polymorphum.";
RL Stand. Genomic Sci. 2:66-76(2010).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR602403-1};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; CP001191; ACI57247.1; -; Genomic_DNA.
DR RefSeq; WP_012559426.1; NC_011369.1.
DR AlphaFoldDB; B5ZVA1; -.
DR STRING; 395492.Rleg2_3985; -.
DR KEGG; rlt:Rleg2_3985; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_001570_5_1_5; -.
DR Proteomes; UP000008330; 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; 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; PTHR24291:SF189; CYTOCHROME P450 4V2; 1.
DR PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 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 {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}.
FT BINDING 410
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:0000256|PIRSR:PIRSR602403-1"
SQ SEQUENCE 466 AA; 52466 MW; 610134E48849DFF6 CRC64;
MDMRPEPFVP PAPLPRTVPP SRLEIIRTIL RNPLELWGEP SYTLPWIKTS FFGQHTLIVN
DPGLIKHVLV DNAGNYRMSD IRQLVLRPIL RDGLLTAEGS VWKRSRKAVA PVFTPRHAQG
FAGQMLRQSE DYAGKYQSEA GPIFDISTDM TELTFAILAD TLFSGEIVTS SGHFADDVNA
LLHRMGRVDP MDLMRAPSWV PRVTRIGGQK VLEKFRAIVR DTMDMRTAKM KADRATAPED
FLTLLLEQAG PDGLTKEEIE DNILTFIGAG HETTARALAW TLYCVSNSPH IREAMETEID
AVLATGAEAV EWLDMMPQTR AAFEETLRLY PPAPSINRAA ISDDSWTSPE GERVELEAGV
TVLIMPWTLH RHELYWDRPR AYMPERFLPE NRGSIGRFQF LPFGAGPRVC IGATFALQEA
VIALAVLMHR YRFDSTDETN PWPVQKLTTQ PQNGLPMRVT PRIISR
//
