ID   E1TEQ9_BURSG            Unreviewed;       574 AA.
AC   E1TEQ9;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE            EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN   OrderedLocusNames=BC1003_4280 {ECO:0000313|EMBL:ADN60214.1};
OS   Burkholderia sp. (strain CCGE1003).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN60214.1};
RN   [1] {ECO:0000313|EMBL:ADN60214.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN60214.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA   Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT   "Complete sequence of chromosome2 of Burkholderia sp. CCGE1003.";
RL   Submitted (SEP-2010) 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; CP002218; ADN60214.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1TEQ9; -.
DR   STRING; 640512.BC1003_4280; -.
DR   KEGG; bgf:BC1003_4280; -.
DR   eggNOG; COG1208; Bacteria.
DR   eggNOG; COG2513; Bacteria.
DR   HOGENOM; CLU_544759_0_0_4; -.
DR   OrthoDB; 9771433at2; -.
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:ADN60214.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          307..417
FT                   /note="MobA-like NTP transferase"
FT                   /evidence="ECO:0000259|Pfam:PF12804"
SQ   SEQUENCE   574 AA;  62149 MW;  0705BE9D5B644709 CRC64;
     MNAREPAFVS ASRSARLRQM LVSNELEFMM EAHNGLSARI VREAGFKAIW GSGLAISAQF
     GVRDNNEASW TQVVGNLEFM ADASDLPILL DGDTGYGNFN NVRRLVRKLE QRGIAGVCIE
     DKQFPKTNSF INGEAQPLAD IDEFCGKIKA GKDSQSDENF SIVARVEALI AGWGMEEALR
     RAEAYRLAGA DAILIHSKLS RPDEILEFAR EWAGRAPLVI VPTKYYSTPT EVFREAGIST
     VIWANHLIRA ATSAMQAVAR EIHTSETLVN VEDRIAAVNE IFRLQDADEY SEAEDRYLSS
     GRAAGSAVVL AASRGKGLEA VTQDRPKVML PVAGKPLLRW LVDAFKKQGV NDITVVGGYR
     ADAIDTAGIK LVVNDRHAET GELASLACAL DKLSGDTVIS YGDLLFRSYI LRDLVESEAA
     FSVVVDSSLT DAENASVRDF AWCSAADDRG LFGNKVVLRH VSSGQEASSA IAAQTPHGRW
     VGLLNVRGAG RERLQTVMRE LQARADFASL DMPALLNALI EAGESIEVQY VHGHWRGVND
     LEDFRRAGDF AHGQTPLAAS VGGADADAAN GAAQ
//