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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//