ID Q3JGT7_BURP1 Unreviewed; 562 AA. AC Q3JGT7; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 87. 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:ABA52482.1}; GN OrderedLocusNames=BURPS1710b_A2065 {ECO:0000313|EMBL:ABA52482.1}; OS Burkholderia pseudomallei (strain 1710b). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320372 {ECO:0000313|EMBL:ABA52482.1, ECO:0000313|Proteomes:UP000002700}; RN [1] {ECO:0000313|EMBL:ABA52482.1, ECO:0000313|Proteomes:UP000002700} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1710b {ECO:0000313|EMBL:ABA52482.1, RC ECO:0000313|Proteomes:UP000002700}; RA Woods D.E., Nierman W.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. 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; CP000125; ABA52482.1; -; Genomic_DNA. DR RefSeq; WP_004525540.1; NC_007435.1. DR AlphaFoldDB; Q3JGT7; -. DR SMR; Q3JGT7; -. DR EnsemblBacteria; ABA52482; ABA52482; BURPS1710b_A2065. DR GeneID; 56531042; -. DR KEGG; bpm:BURPS1710b_A2065; -. DR HOGENOM; CLU_544759_0_0_4; -. DR Proteomes; UP000002700; 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:ABA52482.1}; KW Pyruvate {ECO:0000313|EMBL:ABA52482.1}; 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; 61258 MW; D1E1AEDE5C430884 CRC64; MNAREPNFTE SRSARLRRML TSPSLEFLME AHNGLSARIV REAGFKGIWA 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 //