ID Q2KXP6_BORA1 Unreviewed; 298 AA.
AC Q2KXP6;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Carboxyvinyl-carboxyphosphonate phosphorylmutase {ECO:0000313|EMBL:CAJ48228.1};
DE EC=2.7.8.23 {ECO:0000313|EMBL:CAJ48228.1};
GN OrderedLocusNames=BAV0623 {ECO:0000313|EMBL:CAJ48228.1};
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ48228.1, ECO:0000313|Proteomes:UP000001977};
RN [1] {ECO:0000313|EMBL:CAJ48228.1, ECO:0000313|Proteomes:UP000001977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N {ECO:0000313|EMBL:CAJ48228.1,
RC ECO:0000313|Proteomes:UP000001977};
RX PubMed=16885469; DOI=10.1128/JB.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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DR EMBL; AM167904; CAJ48228.1; -; Genomic_DNA.
DR RefSeq; WP_012416318.1; NC_010645.1.
DR AlphaFoldDB; Q2KXP6; -.
DR STRING; 360910.BAV0623; -.
DR GeneID; 41392532; -.
DR KEGG; bav:BAV0623; -.
DR eggNOG; COG2513; Bacteria.
DR HOGENOM; CLU_027389_3_2_4; -.
DR OrthoDB; 9771433at2; -.
DR Proteomes; UP000001977; Chromosome.
DR GO; GO:0008807; F:carboxyvinyl-carboxyphosphonate phosphorylmutase activity; IEA:UniProtKB-EC.
DR GO; GO:0016833; F:oxo-acid-lyase activity; IEA:UniProt.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR42905:SF16; CARBOXYPHOSPHONOENOLPYRUVATE PHOSPHONOMUTASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_5G07230); 1.
DR PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001977};
KW Transferase {ECO:0000313|EMBL:CAJ48228.1}.
SQ SEQUENCE 298 AA; 32245 MW; 1F005AEA5D33AC90 CRC64;
MNNPRHQFRQ LLKNEPFLVS PGVYDGYSVR LVEAAGFKTA CTSGAAVSNA LLGIADIGVM
GLSENVTHCR HLARSVSIPI TADADTGYGN PVNVYHTVQM FEEAGVAGIN LEDQVSPKRC
GHMPGKDVVS EAEMVKKIEA ACLARRDDDF VIIARTDSLA IEGIEGAVKR ARAYARAGAD
MLFPDAVRTE DDIKRLVDAA GIPVSINMGF GIRNRPTTPL IPLPRLKEIG VKRISLPRML
PAAAIHGMRQ ALAVMQGVIA TGEPADRPDL LVGIEDIMQL MGYEQMRAME KRLTTLDT
//
