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Protein

Phosphoenolpyruvate synthase

Gene

ppsA

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

Functioni

Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.1 Publication

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

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)DescriptionActionsGraphical viewLength
    Active sitei421Tele-phosphohistidine intermediateBy similarity1
    Binding sitei511SubstrateBy similarity1
    Binding sitei578SubstrateBy similarity1
    Metal bindingi680MagnesiumBy similarity1
    Binding sitei680SubstrateBy similarity1
    Binding sitei701Substrate; via carbonyl oxygenBy similarity1
    Binding sitei702Substrate; via amide nitrogenBy similarity1
    Binding sitei703SubstrateBy similarity1
    Metal bindingi704MagnesiumBy similarity1
    Binding sitei704Substrate; via amide nitrogenBy similarity1
    Active sitei751Proton donorBy similarity1

    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

    Keywordsi

    Molecular functionKinase, Transferase
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PEPSYNTH-MONOMER
    MetaCyc:PEPSYNTH-MONOMER
    BRENDAi2.7.9.2 2026
    SABIO-RKiP23538
    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10759 pps

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001470342 – 792Phosphoenolpyruvate synthaseAdd BLAST791

    Proteomic databases

    EPDiP23538
    PaxDbiP23538
    PRIDEiP23538

    2D gel databases

    SWISS-2DPAGEiP23538

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi4262084, 9 interactors
    DIPiDIP-10552N
    IntActiP23538, 10 interactors
    STRINGi316385.ECDH10B_1838

    Structurei

    3D structure databases

    ProteinModelPortaliP23538
    SMRiP23538
    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
    OMAiYRRFVQM
    PhylomeDBiP23538

    Family and domain databases

    Gene3Di3.30.1490.20, 1 hit
    InterProiView protein in InterPro
    IPR013815 ATP_grasp_subdomain_1
    IPR008279 PEP-util_enz_mobile_dom
    IPR006319 PEP_synth
    IPR018274 PEP_util_AS
    IPR000121 PEP_util_C
    IPR023151 PEP_util_CS
    IPR036637 Phosphohistidine_dom_sf
    IPR002192 PPDK_PEP-bd
    IPR015813 Pyrv/PenolPyrv_Kinase-like_dom
    PANTHERiPTHR43030 PTHR43030, 1 hit
    PfamiView protein in Pfam
    PF00391 PEP-utilizers, 1 hit
    PF02896 PEP-utilizers_C, 1 hit
    PF01326 PPDK_N, 1 hit
    PIRSFiPIRSF000854 PEP_synthase, 1 hit
    SUPFAMiSSF51621 SSF51621, 1 hit
    SSF52009 SSF52009, 1 hit
    TIGRFAMsiTIGR01418 PEP_synth, 1 hit
    PROSITEiView protein in PROSITE
    PS00742 PEP_ENZYMES_2, 1 hit
    PS00370 PEP_ENZYMES_PHOS_SITE, 1 hit

    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)DescriptionActionsGraphical viewLength
    Sequence conflicti194 – 195RM → AGL in AAA24319 (Ref. 1) Curated2
    Sequence conflicti341 – 360RSRGQ…GKIIA → AHAVRSWSVIRCIHRVRLSP in AAA24319 (Ref. 1) CuratedAdd BLAST20

    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
    PATRICifig|1411691.4.peg.555

    Similar proteinsi

    Entry informationi

    Entry nameiPPSA_ECOLI
    AccessioniPrimary (citable) accession number: P23538
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: January 23, 2007
    Last modified: March 28, 2018
    This is version 149 of the entry and version 5 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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

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