ID   A0A1G6HYY6_9BURK        Unreviewed;       564 AA.
AC   A0A1G6HYY6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE            EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN   ORFNames=SAMN05216345_10190 {ECO:0000313|EMBL:SDB99400.1};
OS   Cupriavidus sp. YR651.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1855315 {ECO:0000313|EMBL:SDB99400.1, ECO:0000313|Proteomes:UP000198719};
RN   [1] {ECO:0000313|Proteomes:UP000198719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR651 {ECO:0000313|Proteomes:UP000198719};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FMYZ01000001; SDB99400.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6HYY6; -.
DR   STRING; 1855315.SAMN05216345_10190; -.
DR   OrthoDB; 9771433at2; -.
DR   Proteomes; UP000198719; Unassembled WGS sequence.
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:SDB99400.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198719};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          307..417
FT                   /note="MobA-like NTP transferase"
FT                   /evidence="ECO:0000259|Pfam:PF12804"
SQ   SEQUENCE   564 AA;  61635 MW;  0238C38C8F77EEAE CRC64;
     MNAIDPNLLA TSRSARLRQM LLSNDLEFIM EAHNGLSARI VREAGFKGIW ASGLAISAQF
     GVRDNNEASW TQVVDNLEFM ADASDLPILL DGDTGYGNFN NVRRLVRKLE QRGIAGVCIE
     DKIFPKTNSF IGGEQQPLAD IDEFRGKIKA GKDSQADDNF SIVARVEALI AGWGMEEALR
     RAEAYRQAGA DAILIHSKLS KADEIVTFAR EWAGRAPLVI VPTKYYSTPT DVFRKAGISL
     VIWANHLIRV AASSMQAVAK EIHDNETLVN VEDRIATVNE IFRLQDADEY SAAEKIYLTG
     GQAPGSAVVL AAGRGKGLEA LTEDKPKVML PVAGKPLLRW LVDGFKNQGI NDITVVGGYK
     AEAIDAAGIN LVRNDRHAET GELASLACAA DALQNDTVIA YGDLLFRSYI LRDLIDTDAP
     FSVAVDSSET APSNQSVRDF AWCSAADDRD LFGQKITLRK IADERPAGVD APHGRWIGLL
     NVRGEGRARL QAVLADLRRR PDFDKLDLPD LLNALVEAGE EVEVKYVHGH WRGVNDLDDF
     RRAGDFAHTQ TPYALGNTDG EAAR
//