ID A2RYT9_BURM9 Unreviewed; 562 AA.
AC A2RYT9;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN Name=pepM {ECO:0000313|EMBL:ABN00452.1};
GN OrderedLocusNames=BMA10229_1051 {ECO:0000313|EMBL:ABN00452.1};
OS Burkholderia mallei (strain NCTC 10229).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=412022 {ECO:0000313|EMBL:ABN00452.1, ECO:0000313|Proteomes:UP000002283};
RN [1] {ECO:0000313|EMBL:ABN00452.1, ECO:0000313|Proteomes:UP000002283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 10229 {ECO:0000313|EMBL:ABN00452.1,
RC ECO:0000313|Proteomes:UP000002283};
RA DeShazer D., Woods D.E., Nierman W.C.;
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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DR EMBL; CP000545; ABN00452.1; -; Genomic_DNA.
DR RefSeq; WP_004188554.1; NC_008835.1.
DR AlphaFoldDB; A2RYT9; -.
DR GeneID; 56597051; -.
DR KEGG; bml:BMA10229_1051; -.
DR HOGENOM; CLU_544759_0_0_4; -.
DR OMA; DFAWCSA; -.
DR Proteomes; UP000002283; Chromosome II.
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, ECO:0000313|EMBL:ABN00452.1};
KW Pyruvate {ECO:0000313|EMBL:ABN00452.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 307..429
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
SQ SEQUENCE 562 AA; 61316 MW; D1E1AEDE8E5FD884 CRC64;
MNAREPNFTE SRSARLRRML TSPSLEFLME AHNGLSARIV REAGFKDIWA SGLAISAQFG
VRDNNEASWT QVVDVLEFMA DASDLPILLD GDTGYGNFNN VRRLVRKLEQ RGIAGVCIED
KQFPKTNSFI DGERQPLAEI DEFCGKIKAG KDSQSDPDFS IVARVEALIA GWGMDEALRR
ANAYAQAGAD AILIHSKLSR PDEILQFARE WSGRAPLVIV PTKYYSTPTD VFRQAGISTV
IWANHLIRAS ASAMQAVARE IQDSETLVNV EERVASVNEI FRLQDADEYS AAERIYLSSS
ARASSAALVL AASRGNGLEA VTEDKPKVML PVAGKPLLRW LVDGFKKQGV NDITVVGGYR
ADAIDTSGVK LVVNERHAQT GELASLACAA ERLTGDTIIS YGDLLFRSYI LRDLAESEAQ
FSVVVDSSQT QPSNQSVRDF AFCSAADDRG LFGQKAYLRR VSSDASEAAP HGRWIGLLNV
RGAGVARLKA MLGTLQARDD FDALDLPALL NALVDAGEQI EVQYVHGHWR GVNDLDDFRR
AGDFAHGQTP YAEQNAGSGS AR
//