ID I2DW70_9BURK Unreviewed; 561 AA. AC I2DW70; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 24-JAN-2024, entry version 40. DE RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063}; DE EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063}; GN ORFNames=MYA_4542 {ECO:0000313|EMBL:AFJ88896.1}; OS Burkholderia sp. KJ006. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=416344 {ECO:0000313|EMBL:AFJ88896.1, ECO:0000313|Proteomes:UP000010108}; RN [1] {ECO:0000313|EMBL:AFJ88896.1, ECO:0000313|Proteomes:UP000010108} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KJ006 {ECO:0000313|EMBL:AFJ88896.1, RC ECO:0000313|Proteomes:UP000010108}; RX PubMed=22843575; DOI=10.1128/JB.00821-12; RA Kwak M.J., Song J.Y., Kim S.Y., Jeong H., Kang S.G., Kim B.K., Kwon S.K., RA Lee C.H., Yu D.S., Park S.H., Kim J.F.; RT "Complete Genome Sequence of the Endophytic Bacterium Burkholderia sp. RT Strain KJ006."; RL J. Bacteriol. 194:4432-4433(2012). 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; CP003515; AFJ88896.1; -; Genomic_DNA. DR RefSeq; WP_014725080.1; NC_017921.1. DR AlphaFoldDB; I2DW70; -. DR KEGG; buk:MYA_4542; -. DR PATRIC; fig|416344.3.peg.4619; -. DR HOGENOM; CLU_544759_0_0_4; -. DR Proteomes; UP000010108; 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 Pyruvate {ECO:0000313|EMBL:AFJ88896.1}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 307..424 FT /note="MobA-like NTP transferase" FT /evidence="ECO:0000259|Pfam:PF12804" SQ SEQUENCE 561 AA; 61239 MW; FBCF24EC7CB2D772 CRC64; MNAREPNFSE SRSARLRRML VSDQLEFLME AHNGLSARIV REAGFRGIWA SGLAISAQFG VRDNNEASWT QVVDVLEFMA DASDLPILLD GDTGYGNFNN VRRLVKKLEQ RGIAGVCIED KQFPKTNSFI DGERQPLAEI DEFCGKIKAG KDSQSDPDFS IVARVEALIA GWGMDEALRR ANAYAEAGAD AILIHSKLSR PDEILQFARE WSGKAPLVIV PTKYYSTPTD VFRQAGISTV IWANHLIRAS ASAMQAVARE IHENETLINV EDRVASVNEI FRLQDADEYS AAERIYLSSS SRASNAAIVL AASRGKGLEA VTEDKPKVML PVAGKPLLRW LVDGFKKHGV NDITVVGGYR ADAIDTSGIK LVVNERHAQT GELASLACAA ERLTGDTVIS YGDLLFRSYI LRDLAESEAE FSVVVDSSLT ETNQSVRDFA LCSAADDRGL FGQKTYLQRV SSDVAAGAPH GRWIGLLNVR GAGVERLKAM LATLQARADF DTLDIPSLLN ELIAAGEKIE VQYVHGHWRG VNDLEDFRRA GDFAHGQTPL SEPGTTNGGA Q //