ID A4JMZ2_BURVG Unreviewed; 561 AA. AC A4JMZ2; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 84. DE RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063}; DE EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063}; GN OrderedLocusNames=Bcep1808_4687 {ECO:0000313|EMBL:ABO57645.1}; OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia OS (strain R1808)). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=269482 {ECO:0000313|EMBL:ABO57645.1, ECO:0000313|Proteomes:UP000002287}; RN [1] {ECO:0000313|Proteomes:UP000002287} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G4 / LMG 22486 {ECO:0000313|Proteomes:UP000002287}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 2 of Burkholderia vietnamiensis G4."; RL Submitted (MAR-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}. 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; CP000615; ABO57645.1; -; Genomic_DNA. DR AlphaFoldDB; A4JMZ2; -. DR KEGG; bvi:Bcep1808_4687; -. DR eggNOG; COG1208; Bacteria. DR eggNOG; COG2513; Bacteria. DR HOGENOM; CLU_544759_0_0_4; -. DR Proteomes; UP000002287; Chromosome 2. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. 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 Lyase {ECO:0000313|EMBL:ABO57645.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002287}; 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; 61209 MW; FBCF24EC7CAEA772 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 SEPGTANGGA Q //