ID   PPSA_PSEAB              Reviewed;         791 AA.
AC   Q02KR1;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Phosphoenolpyruvate synthase {ECO:0000255|PIRNR:PIRNR000854};
DE            Short=PEP synthase {ECO:0000255|PIRNR:PIRNR000854};
DE            EC=2.7.9.2 {ECO:0000255|PIRNR:PIRNR000854};
DE   AltName: Full=Pyruvate, water dikinase {ECO:0000255|PIRNR:PIRNR000854};
GN   Name=ppsA; OrderedLocusNames=PA14_41670;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT THR-416 AND
RP   TYR-744.
RC   STRAIN=UCBPP-PA14;
RX   PubMed=25096199; DOI=10.1007/s00216-014-8045-8;
RA   Ouidir T., Jarnier F., Cosette P., Jouenne T., Hardouin J.;
RT   "Potential of liquid-isoelectric-focusing protein fractionation to improve
RT   phosphoprotein characterization of Pseudomonas aeruginosa PA14.";
RL   Anal. Bioanal. Chem. 406:6297-6309(2014).
CC   -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC       phosphoenolpyruvate. {ECO:0000255|PIRNR:PIRNR000854}.
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         Evidence={ECO:0000255|PIRNR:PIRNR000854};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|PIRNR:PIRNR000854}.
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.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000255|PIRNR:PIRNR000854}.
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DR   EMBL; CP000438; ABJ10956.1; -; Genomic_DNA.
DR   RefSeq; WP_003098065.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02KR1; -.
DR   SMR; Q02KR1; -.
DR   iPTMnet; Q02KR1; -.
DR   PRIDE; Q02KR1; -.
DR   EnsemblBacteria; ABJ10956; ABJ10956; PA14_41670.
DR   KEGG; pau:PA14_41670; -.
DR   HOGENOM; CLU_007308_6_2_6; -.
DR   OMA; LETWFFL; -.
DR   BioCyc; PAER208963:G1G74-3491-MON; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000653; 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   1: Evidence at protein level;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Pyruvate; Transferase.
FT   CHAIN           1..791
FT                   /note="Phosphoenolpyruvate synthase"
FT                   /id="PRO_0000431474"
FT   ACT_SITE        418
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        748
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         508
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         575
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         677
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         677
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         698
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         699
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         700
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         701
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         701
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         416
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:25096199"
FT   MOD_RES         744
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:25096199"
SQ   SEQUENCE   791 AA;  85817 MW;  F606FB53A0FD5B51 CRC64;
     MVEYVVSLDK LGVHDVEHVG GKNASLGEMI SNLAGAGVSV PGGFATTAQA YRDFLEQSGL
     NDRIHAALDA LDVDDVNALA KTGAQIRQWV MEAEFPARLD SEIRQAFAAL ANGNDNLAVA
     VRSSATAEDL PDASFAGQQE TFLNIRGVDN VIRAAKEVFA SLFNDRAIAY RVHQGFDHKL
     VALSAGVQRM VRSETGTAGV MFTLDTESGF RDVVFITGAY GLGETVVQGA VNPDEFYVHK
     PTLEAGRPAI LRRNLGSKAI KMIYGDEAKA GRSVKVVDVD RADRARFALS DAEVTELAKQ
     AMIIEKHYGR PMDIEWAKDG DDGKLYIVQA RPETVKSRAS ATVMERYLLK EKGTVLVEGR
     AIGQRIGAGP VKVINDVSEM DKVQPGDVLV SDMTDPDWEP VMKRASAIVT NRGGRTCHAA
     IIARELGIPA VVGCGNATQI LQDGQGVTVS CAEGDTGFIF EGELGFDVRK NSVDAMPDLP
     FKIMMNVGNP DRAFDFAQLP NEGVGLARLE FIINRMIGVH PKALLNFAGL PADIKESVEK
     RIAGYPDPVG FYVEKLVEGI STLAAAFWPK KVIVRLSDFK SNEYANLIGG KLYEPEEENP
     MLGFRGASRY ISESFRDCFE LECRALKKVR NEMGLTNVEI MVPFVRTLGE ASQVVELLAG
     NGLKRGENGL KVIMMCELPS NALLADEFLE FFDGFSIGSN DLTQLTLGLD RDSGIVAHLF
     DERNPAVKKL LANAIAACNK AGKYIGICGQ GPSDHPDLAR WLMEQGIESV SLNPDSVLDT
     WFFLAEGQDQ A