ID   A1AR05_PELPD            Unreviewed;       297 AA.
AC   A1AR05;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE            EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN   OrderedLocusNames=Ppro_2167 {ECO:0000313|EMBL:ABK99775.1};
OS   Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC   Desulfuromonadaceae; Pelobacter.
OX   NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK99775.1, ECO:0000313|Proteomes:UP000006732};
RN   [1] {ECO:0000313|EMBL:ABK99775.1, ECO:0000313|Proteomes:UP000006732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2379 / NBRC 103807 / OttBd1
RC   {ECO:0000313|Proteomes:UP000006732};
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   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL   Submitted (OCT-2006) 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; CP000482; ABK99775.1; -; Genomic_DNA.
DR   RefSeq; WP_011736036.1; NC_008609.1.
DR   AlphaFoldDB; A1AR05; -.
DR   STRING; 338966.Ppro_2167; -.
DR   KEGG; ppd:Ppro_2167; -.
DR   eggNOG; COG2513; Bacteria.
DR   HOGENOM; CLU_027389_0_0_7; -.
DR   OrthoDB; 9771433at2; -.
DR   Proteomes; UP000006732; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0050188; F:phosphoenolpyruvate mutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR039556; ICL/PEPM.
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; PF13714; PEP_mutase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Lyase {ECO:0000313|EMBL:ABK99775.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006732}.
SQ   SEQUENCE   297 AA;  32716 MW;  C187A5BE5696CC6F CRC64;
     MARKTTQFRQ LLNSGGIEFL LEAHDGMSAR IVEEAGFKGI WGSGLCISAA MGVRDNNEAS
     WTQVLEVMEF MSDATSIPIL LDADTGYGNF NNVRRLVKKL EQRGVAAMCI EDKLFPKTNS
     FIKGETQPLA DVDEFCGKIK AAKDTQADAD FCVVARVEAL ITGQGQDEAL RRADAYQRAG
     ADAILIHSKK PTAEEILAFM GEWRDTLPVV IVPTTYFNTP PEVFAQAGIS LVIWGNHLMR
     ASITAMQLTA ARINRDRSLS GVEQEIATVK EIFRLQNAQE LAQAEERYLP AHGRPPL
//