ID   PEPM_TETPY              Reviewed;         300 AA.
AC   P33182;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   05-FEB-2025, entry version 91.
DE   RecName: Full=Phosphoenolpyruvate phosphomutase;
DE            Short=PEP mutase;
DE            Short=PEP phosphomutase;
DE            Short=Phosphoenolpyruvate mutase;
DE            EC=5.4.2.9;
DE   Flags: Precursor;
GN   Name=PEPM;
OS   Tetrahymena pyriformis.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=5908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 30331 / GL;
RX   PubMed=1547241; DOI=10.1021/bi00124a021;
RA   Seidel H.M., Pompliano D.L., Knowles J.R.;
RT   "Phosphonate biosynthesis: molecular cloning of the gene for
RT   phosphoenolpyruvate mutase from Tetrahymena pyriformis and overexpression
RT   of the gene product in Escherichia coli.";
RL   Biochemistry 31:2598-2608(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 11-40.
RX   PubMed=3138545; DOI=10.1038/335457a0;
RA   Seidel H.M., Freeman S., Seto H., Knowles J.R.;
RT   "Phosphonate biosynthesis: isolation of the enzyme responsible for the
RT   formation of a carbon-phosphorus bond.";
RL   Nature 335:457-458(1988).
CC   -!- FUNCTION: Formation of a carbon-phosphorus bond by converting
CC       phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphoenolpyruvate + H(+) = 3-phosphonopyruvate;
CC         Xref=Rhea:RHEA:17013, ChEBI:CHEBI:15378, ChEBI:CHEBI:58702,
CC         ChEBI:CHEBI:71402; EC=5.4.2.9;
CC   -!- PATHWAY: Phosphorus metabolism; phosphonate biosynthesis.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC       mutase family. {ECO:0000305}.
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DR   EMBL; M85236; AAA30123.1; -; Genomic_DNA.
DR   PIR; A42204; A42204.
DR   AlphaFoldDB; P33182; -.
DR   SMR; P33182; -.
DR   KEGG; ag:AAA30123; -.
DR   BioCyc; MetaCyc:MONOMER-16742; -.
DR   UniPathway; UPA00960; -.
DR   GO; GO:0050188; F:phosphoenolpyruvate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032923; P:organic phosphonate biosynthetic process; IEA:UniProtKB-UniPathway.
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; 1.
DR   Pfam; PF13714; PEP_mutase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Isomerase.
FT   PROPEP          1..10
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000014458"
FT   CHAIN           11..300
FT                   /note="Phosphoenolpyruvate phosphomutase"
FT                   /id="PRO_0000014459"
FT   ACT_SITE        66
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   300 AA;  33849 MW;  19D825A69D60AD39 CRC64;
     MLANSLKSFF SSTRKTTQLK NMIQSKDLSF IMEAHNGLSA AIVEETGFKG IWGSGLSISA
     AMGVRDSNEA SYTQVLEVLE FMSDRTKIPI LLDGDTGYGN YNNARRLVKK LEQRSIAGVC
     LEDKIFPKRN SLLDDGRQEL APINEFVAKI KACKDTQQDA DFQVVARVEA FIAGWGLEEA
     LKRAEAYRNA GADAILMHSK LKEPSEIEAF MKEWKNRSPV IIVPTNYHTV PTDTFRKWGV
     NMVIWANHNM RACVSAMQET SRRIYEDESL VNVEPKVAKV KEVFRLQGED ELKQADKKYL
//