ID Q63MP0_BURPS Unreviewed; 303 AA.
AC Q63MP0;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN OrderedLocusNames=BPSS0610 {ECO:0000313|EMBL:CAH38067.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH38067.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH38067.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH38067.1,
RC ECO:0000313|Proteomes:UP000000605};
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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DR EMBL; BX571966; CAH38067.1; -; Genomic_DNA.
DR RefSeq; WP_004523200.1; NZ_CP009537.1.
DR RefSeq; YP_110631.1; NC_006351.1.
DR AlphaFoldDB; Q63MP0; -.
DR STRING; 272560.BPSS0610; -.
DR GeneID; 56530939; -.
DR KEGG; bps:BPSS0610; -.
DR PATRIC; fig|272560.51.peg.6792; -.
DR eggNOG; COG2513; Bacteria.
DR Proteomes; UP000000605; Chromosome 2.
DR GO; GO:0050188; F:phosphoenolpyruvate mutase activity; IEA:UniProtKB-EC.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR012698; PEnolPyrv_PMutase_core.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR02320; PEP_mutase; 1.
DR PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR42905:SF7; PHOSPHOENOLPYRUVATE PHOSPHOMUTASE-RELATED; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Reference proteome {ECO:0000313|Proteomes:UP000000605}.
SQ SEQUENCE 303 AA; 33443 MW; EDD3DDDA3E3098AD CRC64;
MPIRELISAP ITNEQRRRSF KEKLATGRAL RFIESHSPIS AMISEKVYVA HGASQSEFDG
FWSSSLTDST LRGRPDIEIL DIASRLANVQ HIFDVTTKPL IIDGDTGGKP EHFALNVQSL
ERSGVSAVII EDKTGLKKNS LLGNDVIQHQ ESIEDFCEKI RVGKAAQITD DFQIIARVES
LILDKGMPDA LARAAAYCEA GADGVMIHSR KKDADEVIEF AQRFRACRRD AYLVCVPTSF
NAISFSELAR HFSVVIYANH LLRAAYPAML AVAEGILAHG RTLEIEERCL PVNEILKLIP
GTA
//
