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Database: UniProt/TrEMBL
Entry: Q63MY9_BURPS
LinkDB: Q63MY9_BURPS
Original site: Q63MY9_BURPS 
ID   Q63MY9_BURPS            Unreviewed;       544 AA.
AC   Q63MY9;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE            EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN   OrderedLocusNames=BPSS0509 {ECO:0000313|EMBL:CAH37966.1};
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH37966.1, ECO:0000313|Proteomes:UP000000605};
RN   [1] {ECO:0000313|EMBL:CAH37966.1, ECO:0000313|Proteomes:UP000000605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243 {ECO:0000313|EMBL:CAH37966.1,
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; CAH37966.1; -; Genomic_DNA.
DR   RefSeq; YP_110530.1; NC_006351.1.
DR   AlphaFoldDB; Q63MY9; -.
DR   STRING; 272560.BPSS0509; -.
DR   KEGG; bps:BPSS0509; -.
DR   PATRIC; fig|272560.6.peg.4521; -.
DR   eggNOG; COG1208; Bacteria.
DR   eggNOG; COG2513; Bacteria.
DR   OMA; DFAWCSA; -.
DR   Proteomes; UP000000605; Chromosome 2.
DR   GO; GO:0050188; F:phosphoenolpyruvate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   CDD; cd02523; PC_cytidylyltransferase; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR039556; ICL/PEPM.
DR   InterPro; IPR025877; MobA-like_NTP_Trfase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
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; PF12804; NTP_transf_3; 1.
DR   Pfam; PF13714; PEP_mutase; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          289..411
FT                   /note="MobA-like NTP transferase"
FT                   /evidence="ECO:0000259|Pfam:PF12804"
SQ   SEQUENCE   544 AA;  59084 MW;  99050DCBD6CCA67F CRC64;
     MLTSPSLEFL MEAHNGLSAR IVREAGFKGI WASGLAISAQ FGVRDNNEAS WTQVVDVLEF
     MADASDLPIL LDGDTGYGNF NNVRRLVRKL EQRGIAGVCI EDKQFPKTNS FIDGERQPLA
     EIDEFCGKIK AGKDSQSDPD FSIVARVEAL IAGWGMDEAL RRANAYAQAG ADAILIHSKL
     SRPDEILQFA REWSGRAPLV IVPTKYYSTP TDVFRQAGIS TVIWANHLIR ASASAMQAVA
     REIQDSETLV NVEERVASVN EIFRLQDADE YSAAERIYLS SSARASSAAL VLAASRGNGL
     EAVTEDKPKV MLPVAGKPLL RWLVDGFKKQ GVNDITVVGG YRADAIDTSG VKLVVNERHA
     QTGELASLAC AAERLTGDTI ISYGDLLFRS YILRDLAESE AQFSVVVDSS QTQPSNQSVR
     DFAFCSAADD RGLFGQKAYL RRVSSDASEA APHGRWIGLL NVRGAGVARL KAMLGTLQAR
     DDFDALDLPA LLNALVDAGE QIEVQYVHGH WRGVNDLDDF RRAGDFAHGQ TPYAEQNAGS
     GSAR
//
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