ID   PEPM_STRVT              Reviewed;         313 AA.
AC   O86937; Q4JFE7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   24-JAN-2024, entry version 83.
DE   RecName: Full=Phosphoenolpyruvate phosphomutase;
DE            Short=PEP mutase;
DE            Short=PEP phosphomutase;
DE            Short=Phosphoenolpyruvate mutase;
DE            EC=5.4.2.9;
GN   Name=ppm;
OS   Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS   Tue 494).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=591159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494;
RX   PubMed=9673017; DOI=10.1111/j.1574-6968.1998.tb13039.x;
RA   Schwartz D., Recktenwald J., Pelzer S., Wohlleben W.;
RT   "Isolation and characterization of the PEP-phosphomutase and the
RT   phosphonopyruvate decarboxylase genes from the phosphinothricin tripeptide
RT   producer Streptomyces viridochromogenes Tu494.";
RL   FEMS Microbiol. Lett. 163:149-157(1998).
CC   -!- FUNCTION: Formation of a carbon-phosphorus bond by converting
CC       phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + phosphoenolpyruvate = 3-phosphonopyruvate;
CC         Xref=Rhea:RHEA:17013, ChEBI:CHEBI:15378, ChEBI:CHEBI:58702,
CC         ChEBI:CHEBI:71402; EC=5.4.2.9;
CC   -!- PATHWAY: Secondary metabolite biosynthesis; bialaphos biosynthesis.
CC       {ECO:0000305|PubMed:9673017}.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC       mutase family. {ECO:0000305}.
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; X65195; CAJ14044.1; -; Genomic_DNA.
DR   AlphaFoldDB; O86937; -.
DR   SMR; O86937; -.
DR   STRING; 591159.SSQG_01039; -.
DR   eggNOG; COG2513; Bacteria.
DR   UniPathway; UPA00197; -.
DR   GO; GO:0050188; F:phosphoenolpyruvate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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   Antibiotic biosynthesis; Isomerase.
FT   CHAIN           1..313
FT                   /note="Phosphoenolpyruvate phosphomutase"
FT                   /id="PRO_0000068826"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        69
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   313 AA;  33477 MW;  64717D362836E935 CRC64;
     MNATERPGSD GTGSPESVGS RLKNLLHGPG TCQLMGVHDG LSARIAVAEG FEALWASGLC
     MSTARGVRDS DEASWTELLT LVGTMTEAAP GAPVLVDGDT GYGNFNTARP SPPAPSCLGA
     AGVCFEDKVF PKMNSFFGDG HQLAPIGEFS GKIKACKDTQ RDPGFVVVAR TEALISNLPM
     EEALTRAHAY VEAVADGLFI HSRMSTPQQI AEFMRQWDGS APILIAPTTY HRPSLDDFAA
     LGIAGCIWAN HSMRAAFSAM RDVCQQIRAD RGIFGVEERV APLKEIFGLL DYESLEQDEN
     RYTQAPDLAP VQG
//