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
//