ID   PPSA_ENTAG              Reviewed;          61 AA.
AC   O54457;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Phosphoenolpyruvate synthase;
DE            Short=PEP synthase;
DE            EC=2.7.9.2;
DE   AltName: Full=Pyruvate, water dikinase;
DE   Flags: Fragment;
GN   Name=ppsA;
OS   Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX   NCBI_TaxID=549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9422601; DOI=10.1128/jb.180.1.119-127.1998;
RA   Subramaniam P.S., Xie G., Xia T., Jensen R.A.;
RT   "Substrate ambiguity of 3-deoxy-D-manno-octulosonate 8-phosphate synthase
RT   from Neisseria gonorrhoeae in the context of its membership in a protein
RT   family containing a subset of 3-deoxy-D-arabino-heptulosonate 7-phosphate
RT   synthases.";
RL   J. Bacteriol. 180:119-127(1998).
CC   -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC       phosphoenolpyruvate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:11364, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.2;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- DOMAIN: The N-terminal domain contains the ATP/Pi binding site, the
CC       central domain the pyrophosphate/phosphate carrier histidine, and the
CC       C-terminal domain the pyruvate binding site. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The reaction takes place in three steps, mediated by a
CC       phosphocarrier histidine residue located on the surface of the central
CC       domain. The two first partial reactions are catalyzed at an active site
CC       located on the N-terminal domain, and the third partial reaction is
CC       catalyzed at an active site located on the C-terminal domain. For
CC       catalytic turnover, the central domain swivels from the concave surface
CC       of the N-terminal domain to that of the C-terminal domain (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
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DR   EMBL; U93355; AAB96398.1; -; Genomic_DNA.
DR   AlphaFoldDB; O54457; -.
DR   SMR; O54457; -.
DR   STRING; 549.BW31_01628; -.
DR   eggNOG; COG0574; Bacteria.
DR   eggNOG; COG1080; Bacteria.
DR   UniPathway; UPA00138; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR006319; PEP_synth.
DR   InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR   PANTHER; PTHR43030; PTHR43030; 1.
DR   Pfam; PF01326; PPDK_N; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Transferase.
FT   CHAIN           1..>61
FT                   /note="Phosphoenolpyruvate synthase"
FT                   /id="PRO_0000147035"
FT   NON_TER         61
SQ   SEQUENCE   61 AA;  6605 MW;  77AF7475B7A1CAD9 CRC64;
     MSSKGEQPLV LWYNQLGMHD VDRVGGKNPS LGEMITNLSS LGVSVPNGFA TTSYAFNLFL
     D