ID   B2JNA5_PARP8            Unreviewed;       568 AA.
AC   B2JNA5;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE            EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN   OrderedLocusNames=Bphy_3822 {ECO:0000313|EMBL:ACC72953.1};
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC72953.1, ECO:0000313|Proteomes:UP000001192};
RN   [1] {ECO:0000313|Proteomes:UP000001192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC   {ECO:0000313|Proteomes:UP000001192};
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA   James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA   Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA   Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT   range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC       mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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DR   EMBL; CP001044; ACC72953.1; -; Genomic_DNA.
DR   RefSeq; WP_012403126.1; NZ_CADFGH010000016.1.
DR   AlphaFoldDB; B2JNA5; -.
DR   STRING; 391038.Bphy_3822; -.
DR   KEGG; bph:Bphy_3822; -.
DR   eggNOG; COG1208; Bacteria.
DR   eggNOG; COG2513; Bacteria.
DR   HOGENOM; CLU_544759_0_0_4; -.
DR   OrthoDB; 9771433at2; -.
DR   Proteomes; UP000001192; 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:ACC72953.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001192};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          307..421
FT                   /note="MobA-like NTP transferase"
FT                   /evidence="ECO:0000259|Pfam:PF12804"
SQ   SEQUENCE   568 AA;  62093 MW;  03CEEFEA611BDFA2 CRC64;
     MNAREPSFTT LSRSARLRQM LTSNELEFLM EAHNGISARI VREAGFKGIW GSGLAISAQY
     GVRDNNEASW TQVVDTLEFM ADASDLPILL DGDTGYGNFN NVRRLVRKLE QRGIAGVCIE
     DKVFPKTNSF IKGEAQPLAD IDEFCGKIKA GKDSQTDEDF SIVARVEALI AGWGMEEALK
     RAEAYRQAGA DAILIHSKLS RPDEILEFAR EWAGRGPLVI VPTKYYSTPT EVFRKAGIST
     VIWANHQIRA ATSAMQAVVK EIYESQTLVN VEDRIATVNE IFRLQNADEY SEAEERYLSS
     SRAAGSAVVL AASRGAGLEA VTTDRPKVML PIAGKPLLRW LVDAFKKQGV NDITVVGGYR
     ADAIDTAGIK LVVNERHEQT GELASLACAI DNLQNDTLIS YGDLLFRSYI VRDLVESEAP
     FSVVVDSTTI DETGAANQSV RDFAWCSAGD DRGLFGNKVL LRRVSNNEAD LHGAAPNGRW
     IGLLNVRGGG RERLQAVMST LRARPDFDSL DMPALLNALL EAGEEIEVQY VHGHWRGVND
     LEDFRRAGDF AHEATPLAKG DAAGGAAQ
//