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Protein

Phosphoenolpyruvate synthase

Gene

ppsA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.1 Publication

Catalytic activityi

ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate.2 Publications

Cofactori

Mg2+1 Publication

Enzyme regulationi

Activated by a Pi-dependent pyrophosphorylation and inactivated by an ADP-dependent phosphorylation on a regulatory threonine. Both reactions are mediated by the bifunctional serine/threonine kinase and phosphorylase PpsR.1 Publication

Kineticsi

  1. KM=0.083 mM for pyruvate1 Publication
  2. KM=0.028 mM for ATP1 Publication
  3. KM=10.4 mM for phosphate1 Publication

    Pathwayi: gluconeogenesis

    This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei421 – 4211Tele-phosphohistidine intermediateBy similarity
    Binding sitei511 – 5111SubstrateBy similarity
    Binding sitei578 – 5781SubstrateBy similarity
    Metal bindingi680 – 6801MagnesiumBy similarity
    Binding sitei680 – 6801SubstrateBy similarity
    Binding sitei701 – 7011Substrate; via carbonyl oxygenBy similarity
    Binding sitei702 – 7021Substrate; via amide nitrogenBy similarity
    Binding sitei703 – 7031SubstrateBy similarity
    Metal bindingi704 – 7041MagnesiumBy similarity
    Binding sitei704 – 7041Substrate; via amide nitrogenBy similarity
    Active sitei751 – 7511Proton donorBy similarity

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • magnesium ion binding Source: EcoCyc
    • pyruvate, water dikinase activity Source: EcoCyc

    GO - Biological processi

    • gluconeogenesis Source: EcoCyc
    • pyruvate metabolic process Source: InterPro
    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PEPSYNTH-MONOMER.
    ECOL316407:JW1692-MONOMER.
    MetaCyc:PEPSYNTH-MONOMER.
    BRENDAi2.7.9.2. 2026.
    SABIO-RKP23538.
    UniPathwayiUPA00138.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoenolpyruvate synthase (EC:2.7.9.2)
    Short name:
    PEP synthase
    Alternative name(s):
    Pyruvate, water dikinase
    Gene namesi
    Name:ppsA
    Synonyms:pps
    Ordered Locus Names:b1702, JW1692
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10759. pps.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 792791Phosphoenolpyruvate synthasePRO_0000147034Add
    BLAST

    Proteomic databases

    EPDiP23538.
    PaxDbiP23538.
    PRIDEiP23538.

    2D gel databases

    SWISS-2DPAGEP23538.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    DIPiDIP-10552N.
    IntActiP23538. 6 interactions.
    STRINGi511145.b1702.

    Structurei

    3D structure databases

    ProteinModelPortaliP23538.
    SMRiP23538. Positions 10-788.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    The N-terminal domain contains the ATP/Pi binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.By similarity

    Sequence similaritiesi

    Belongs to the PEP-utilizing enzyme family.Curated

    Phylogenomic databases

    eggNOGiENOG4108HRN. Bacteria.
    COG0574. LUCA.
    HOGENOMiHOG000230913.
    InParanoidiP23538.
    KOiK01007.
    OMAiMVIEKHY.
    OrthoDBiEOG632CZ4.
    PhylomeDBiP23538.

    Family and domain databases

    Gene3Di3.20.20.60. 1 hit.
    3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.50.30.10. 1 hit.
    InterProiIPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR008279. PEP-util_enz_mobile_dom.
    IPR006319. PEP_synth.
    IPR018274. PEP_util_AS.
    IPR000121. PEP_util_C.
    IPR023151. PEP_util_CS.
    IPR002192. PPDK_PEP-bd.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view]
    PfamiPF00391. PEP-utilizers. 1 hit.
    PF02896. PEP-utilizers_C. 1 hit.
    PF01326. PPDK_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000854. PEP_synthase. 1 hit.
    SUPFAMiSSF51621. SSF51621. 1 hit.
    SSF52009. SSF52009. 1 hit.
    TIGRFAMsiTIGR01418. PEP_synth. 1 hit.
    PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
    PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P23538-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSNNGSSPLV LWYNQLGMND VDRVGGKNAS LGEMITNLSG MGVSVPNGFA
    60 70 80 90 100
    TTADAFNQFL DQSGVNQRIY ELLDKTDIDD VTQLAKAGAQ IRQWIIDTPF
    110 120 130 140 150
    QPELENAIRE AYAQLSADDE NASFAVRSSA TAEDMPDASF AGQQETFLNV
    160 170 180 190 200
    QGFDAVLVAV KHVFASLFND RAISYRVHQG YDHRGVALSA GVQRMVRSDL
    210 220 230 240 250
    ASSGVMFSID TESGFDQVVF ITSAWGLGEM VVQGAVNPDE FYVHKPTLAA
    260 270 280 290 300
    NRPAIVRRTM GSKKIRMVYA PTQEHGKQVK IEDVPQEQRD IFSLTNEEVQ
    310 320 330 340 350
    ELAKQAVQIE KHYGRPMDIE WAKDGHTGKL FIVQARPETV RSRGQVMERY
    360 370 380 390 400
    TLHSQGKIIA EGRAIGHRIG AGPVKVIHDI SEMNRIEPGD VLVTDMTDPD
    410 420 430 440 450
    WEPIMKKASA IVTNRGGRTC HAAIIARELG IPAVVGCGDA TERMKDGENV
    460 470 480 490 500
    TVSCAEGDTG YVYAELLEFS VKSSSVETMP DLPLKVMMNV GNPDRAFDFA
    510 520 530 540 550
    CLPNEGVGLA RLEFIINRMI GVHPRALLEF DDQEPQLQNE IREMMKGFDS
    560 570 580 590 600
    PREFYVGRLT EGIATLGAAF YPKRVIVRLS DFKSNEYANL VGGERYEPDE
    610 620 630 640 650
    ENPMLGFRGA GRYVSDSFRD CFALECEAVK RVRNDMGLTN VEIMIPFVRT
    660 670 680 690 700
    VDQAKAVVEE LARQGLKRGE NGLKIIMMCE IPSNALLAEQ FLEYFDGFSI
    710 720 730 740 750
    GSNDMTQLAL GLDRDSGVVS ELFDERNDAV KALLSMAIRA AKKQGKYVGI
    760 770 780 790
    CGQGPSDHED FAAWLMEEGI DSLSLNPDTV VQTWLSLAEL KK
    Length:792
    Mass (Da):87,435
    Last modified:January 23, 2007 - v5
    Checksum:iDBBAB0BA9B9F7DD9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti194 – 1952RM → AGL in AAA24319 (Ref. 1) Curated
    Sequence conflicti341 – 36020RSRGQ…GKIIA → AHAVRSWSVIRCIHRVRLSP in AAA24319 (Ref. 1) CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M69116 Genomic DNA. Translation: AAA24319.1.
    X59381 Genomic DNA. Translation: CAA42024.1.
    U00096 Genomic DNA. Translation: AAC74772.1.
    AP009048 Genomic DNA. Translation: BAA15471.1.
    PIRiS20554.
    RefSeqiNP_416217.1. NC_000913.3.
    WP_000069375.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74772; AAC74772; b1702.
    BAA15471; BAA15471; BAA15471.
    GeneIDi946209.
    KEGGiecj:JW1692.
    eco:b1702.
    PATRICi32118710. VBIEscCol129921_1773.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M69116 Genomic DNA. Translation: AAA24319.1.
    X59381 Genomic DNA. Translation: CAA42024.1.
    U00096 Genomic DNA. Translation: AAC74772.1.
    AP009048 Genomic DNA. Translation: BAA15471.1.
    PIRiS20554.
    RefSeqiNP_416217.1. NC_000913.3.
    WP_000069375.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP23538.
    SMRiP23538. Positions 10-788.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-10552N.
    IntActiP23538. 6 interactions.
    STRINGi511145.b1702.

    2D gel databases

    SWISS-2DPAGEP23538.

    Proteomic databases

    EPDiP23538.
    PaxDbiP23538.
    PRIDEiP23538.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74772; AAC74772; b1702.
    BAA15471; BAA15471; BAA15471.
    GeneIDi946209.
    KEGGiecj:JW1692.
    eco:b1702.
    PATRICi32118710. VBIEscCol129921_1773.

    Organism-specific databases

    EchoBASEiEB0752.
    EcoGeneiEG10759. pps.

    Phylogenomic databases

    eggNOGiENOG4108HRN. Bacteria.
    COG0574. LUCA.
    HOGENOMiHOG000230913.
    InParanoidiP23538.
    KOiK01007.
    OMAiMVIEKHY.
    OrthoDBiEOG632CZ4.
    PhylomeDBiP23538.

    Enzyme and pathway databases

    UniPathwayiUPA00138.
    BioCyciEcoCyc:PEPSYNTH-MONOMER.
    ECOL316407:JW1692-MONOMER.
    MetaCyc:PEPSYNTH-MONOMER.
    BRENDAi2.7.9.2. 2026.
    SABIO-RKP23538.

    Miscellaneous databases

    PROiP23538.

    Family and domain databases

    Gene3Di3.20.20.60. 1 hit.
    3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.50.30.10. 1 hit.
    InterProiIPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR008279. PEP-util_enz_mobile_dom.
    IPR006319. PEP_synth.
    IPR018274. PEP_util_AS.
    IPR000121. PEP_util_C.
    IPR023151. PEP_util_CS.
    IPR002192. PPDK_PEP-bd.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view]
    PfamiPF00391. PEP-utilizers. 1 hit.
    PF02896. PEP-utilizers_C. 1 hit.
    PF01326. PPDK_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000854. PEP_synthase. 1 hit.
    SUPFAMiSSF51621. SSF51621. 1 hit.
    SSF52009. SSF52009. 1 hit.
    TIGRFAMsiTIGR01418. PEP_synth. 1 hit.
    PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
    PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The cloning and sequence of the E. coli pps gene."
      Holzschu D.L., McElver J.A., Liao C.C., Berry A.
      Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Cloning and nucleotide sequence of the Escherichia coli K-12 ppsA gene, encoding PEP synthase."
      Niersbach M., Kreuzaler F., Geerse R.H., Postma P.W., Hirsch H.J.
      Mol. Gen. Genet. 231:332-336(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21.
      Strain: K12.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "The mechanism of the phosphoenolpyruvate synthase reaction."
      Cooper R.A., Kornberg H.L.
      Biochim. Biophys. Acta 141:211-213(1967) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    7. "Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent metal ions."
      Berman K.M., Cohn M.
      J. Biol. Chem. 245:5309-5318(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
    8. "Phosphoenolypyruvate synthetase of Escherichia coli: molecular weight, subunit composition, and identification of phosphohistidine in phosphoenzyme intermediate."
      Narindrasorasak S., Bridger W.A.
      J. Biol. Chem. 252:3121-3127(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHOINTERMEDIATE OF REACTION, SUBUNIT, AMINO-ACID COMPOSITION.
    9. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    10. "Cloning and characterization of Escherichia coli DUF299: a bifunctional ADP-dependent kinase--Pi-dependent pyrophosphorylase from bacteria."
      Burnell J.N.
      BMC Biochem. 11:1-1(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.

    Entry informationi

    Entry nameiPPSA_ECOLI
    AccessioniPrimary (citable) accession number: P23538
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: January 23, 2007
    Last modified: March 16, 2016
    This is version 135 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain (By similarity).By similarity

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.