ID   PPSA_HELPJ              Reviewed;         812 AA.
AC   Q9ZMV4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Phosphoenolpyruvate synthase;
DE            Short=PEP synthase;
DE            EC=2.7.9.2;
DE   AltName: Full=Pyruvate, water dikinase;
GN   Name=ppsA; OrderedLocusNames=jhp_0111;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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; AE001439; AAD05690.1; -; Genomic_DNA.
DR   PIR; E71972; E71972.
DR   RefSeq; WP_001269113.1; NC_000921.1.
DR   AlphaFoldDB; Q9ZMV4; -.
DR   SMR; Q9ZMV4; -.
DR   STRING; 85963.jhp_0111; -.
DR   EnsemblBacteria; AAD05690; AAD05690; jhp_0111.
DR   KEGG; hpj:jhp_0111; -.
DR   eggNOG; COG0574; Bacteria.
DR   eggNOG; COG1080; Bacteria.
DR   OMA; LETWFFL; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000804; Chromosome.
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; 3.20.20.60; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR006319; PEP_synth.
DR   InterPro; IPR018274; PEP_util_AS.
DR   InterPro; IPR000121; PEP_util_C.
DR   InterPro; IPR023151; PEP_util_CS.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR43030; PTHR43030; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   Pfam; PF01326; PPDK_N; 1.
DR   PIRSF; PIRSF000854; PEP_synthase; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   SUPFAM; SSF52009; SSF52009; 1.
DR   TIGRFAMs; TIGR01418; PEP_synth; 1.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..812
FT                   /note="Phosphoenolpyruvate synthase"
FT                   /id="PRO_0000147037"
FT   ACT_SITE        430
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        761
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         520
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         588
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         690
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         690
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         711
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         712
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         713
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         714
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         714
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   812 AA;  91291 MW;  A088D459B3E47512 CRC64;
     MRYIKFFKEL NNKNVNLVGG KNASIGEMFQ ELVPIGIKVP DGFAITSEAY WYLLEQGGAK
     QKIIELLENV DATEIDVLKI RSKQIRELIF GTPFPSDLRD EIFQAYEILS QQYHMKEADV
     AVRSSATAED LPDASFAGQQ DTYLNIKGKT ELIHYIKSCL ASLFTDRAIS YRASRGFDHL
     KVALSVGVQK MVRADKGSAG VMFSIDTETG FKDAVFITSA WGLGENVVGG TINPDEFYVF
     KPTLEQNKRP IIKRQLGNKT QKMVYAPRGS EHPTRNIKTT KKEWQSFSLS DEDVLILAKY
     AIEIEKHYSK EAKQYRPMDI EWAKDGESGE IFIVQARPET VQSQKTKEEN QVFEKFKFKN
     PNEKKEIILQ GRAIGSKIGS GKVRIINDLE HMNSFKEGEI LVTDNTDPDW EPCMKKASAV
     ITNRGGRTCH AAIVAREIGV PAIVGVSGAT DSLYTGMEIT VSCAEGEEGY VYAGIYEHEI
     ERVELSNMQE TQTKIYINIG NPEKAFSFSQ LPNHGVGLAR MEMIILNQIK AHPLALVDLH
     HKKSVKEKNE IENLMAGYAN PKDFFVKKIA EGIGMISAAF YPKPVIVRTS DFKSNEYMRM
     LGGSSYEPNE ENPMLGYRGA SRYYSESYNE AFSWECEALA LVREEMGLTN MKVMIPFLRT
     IEEGKKVLEI LRKNNLESGK NGLEIYIMCE LPVNVILADD FLSLFDGFSI GSNDLTQLTL
     GVDRDSELVS HVFDERNEAM LKMFKKAIEA CKRHNKYCGI CGQAPSDYPE VTEFLVKEGI
     TSISLNPDSV IPTWNAVAKL EKELKDHGLT AR