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Protein

Phosphoenolpyruvate synthase

Gene

ppsA

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
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.1 Publication

Cofactori

Kineticsi

  1. KM=0.11 mM for pyruvate1 Publication
  2. KM=0.40 mM for phosphoenolpyruvate1 Publication
  3. KM=0.39 mM for ATP1 Publication
  4. KM=1.00 mM for AMP1 Publication
  5. KM=38.4 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 sitei442 – 4421Tele-phosphohistidine intermediateBy similarity
    Binding sitei540 – 5401SubstrateBy similarity
    Binding sitei587 – 5871SubstrateBy similarity
    Metal bindingi684 – 6841MagnesiumBy similarity
    Binding sitei684 – 6841SubstrateBy similarity
    Binding sitei706 – 7061Substrate; via carbonyl oxygenBy similarity
    Binding sitei707 – 7071Substrate; via amide nitrogenBy similarity
    Binding sitei708 – 7081SubstrateBy similarity
    Metal bindingi709 – 7091MagnesiumBy similarity
    Binding sitei709 – 7091Substrate; via amide nitrogenBy similarity
    Active sitei756 – 7561Proton donorBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi2.7.9.2. 5243.
    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
    Ordered Locus Names:PF0043
    OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
    Taxonomic identifieri186497 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    Proteomesi
    • UP000001013 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 817816Phosphoenolpyruvate synthasePRO_0000147044Add
    BLAST

    Proteomic databases

    PRIDEiP42850.

    Interactioni

    Subunit structurei

    Homooctamer.1 Publication

    Protein-protein interaction databases

    STRINGi186497.PF0043.

    Structurei

    3D structure databases

    ProteinModelPortaliP42850.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi809 – 8157Poly-Glu

    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

    eggNOGiarCOG01111. Archaea.
    COG0574. LUCA.
    HOGENOMiHOG000230912.
    KOiK01007.
    OMAiQIRQWIM.

    Family and domain databases

    Gene3Di3.20.20.60. 1 hit.
    3.30.1490.20. 2 hits.
    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.

    P42850-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAYRFIKWFE ELSKNDVPLV GGKGANLGEM TNAGIPVPPG FCVTAEAYKY
    60 70 80 90 100
    FVENVKVSKE DVKRILGEKV NKGTISEVLA QAPDEPRPLQ DWIMDIISKT
    110 120 130 140 150
    DVDDSKMLQE NTEAIRTLIK SLDMPSEIAE EIKQAYKELS QRFGQEEVYV
    160 170 180 190 200
    AVRSSATAED LPEASFAGQQ ETYLDVLGAD DVIDKVKRCW ASLWTARATF
    210 220 230 240 250
    YRAKQGFDHS KVYLSAVVQK MVNSEKSGVM FTANPVTNNR NEIMINASWG
    260 270 280 290 300
    LGEAVVSGAV TPDEYIVEKG TWKIKEKVIA KKEVMVIRNP ETGRGTVMVK
    310 320 330 340 350
    VAEYLGPEWV EKQVLTDEQI IEVAKMGQKI EDHYGWPQDI EWAYDKDDGK
    360 370 380 390 400
    LYIVQSRPIT TLKEEATAEE AEEVEEAEVI LKGLGASPGI GAGRVVVIFD
    410 420 430 440 450
    ASEIDKVKEG DILVTTMTNP DMVPAMKRAA AIVTDEGGRT SHAAIVSREL
    460 470 480 490 500
    GIPCVVGTKE ATKKLKTGMY VTVDGTRGLV YKGIVKSLVK KKEEAKAEGG
    510 520 530 540 550
    QVVVAGAPLV TGTMVKVNVS MPEVAERAAA TGADGVGLLR AEHMILSIGQ
    560 570 580 590 600
    HPIKFIKEGK EEELVEKLAE GIEKVAAAFY PRPVWYRTLD APTNEFREMP
    610 620 630 640 650
    GGEDEPEERN PMLGWRGIRR GLDQPELLRA EFKAIKKVVE KGYNNIGVML
    660 670 680 690 700
    PLVSHPEQIR EAKRIAREVG LEPHKDVAWG VMIEVPAAAI IIEDLIKEGI
    710 720 730 740 750
    DFVSFGTNDL TQYTLAIDRD NERVAKLYDE THPAVLKLIK HVIKVCKRYG
    760 770 780 790 800
    VETSICGQAG SDPKMARILV RLGIDSISAN PDAVQLIRQV VAQEERKLML
    810
    EAARKQLFEE EEEEELF
    Length:817
    Mass (Da):90,485
    Last modified:April 3, 2002 - v3
    Checksum:iDA3A7A3CF13C614F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81W → G AA sequence (PubMed:11133966).Curated
    Sequence conflicti747 – 7471K → Q in AAA81512 (PubMed:7828869).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U08376 Genomic DNA. Translation: AAA81512.1.
    X80819 Genomic DNA. Translation: CAA56785.1.
    AE009950 Genomic DNA. Translation: AAL80167.1.
    PIRiJC4176.
    RefSeqiWP_011011155.1. NC_003413.1.

    Genome annotation databases

    EnsemblBacteriaiAAL80167; AAL80167; PF0043.
    GeneIDi1467872.
    KEGGipfu:PF0043.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U08376 Genomic DNA. Translation: AAA81512.1.
    X80819 Genomic DNA. Translation: CAA56785.1.
    AE009950 Genomic DNA. Translation: AAL80167.1.
    PIRiJC4176.
    RefSeqiWP_011011155.1. NC_003413.1.

    3D structure databases

    ProteinModelPortaliP42850.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi186497.PF0043.

    Proteomic databases

    PRIDEiP42850.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAL80167; AAL80167; PF0043.
    GeneIDi1467872.
    KEGGipfu:PF0043.

    Phylogenomic databases

    eggNOGiarCOG01111. Archaea.
    COG0574. LUCA.
    HOGENOMiHOG000230912.
    KOiK01007.
    OMAiQIRQWIM.

    Enzyme and pathway databases

    UniPathwayiUPA00138.
    BRENDAi2.7.9.2. 5243.

    Family and domain databases

    Gene3Di3.20.20.60. 1 hit.
    3.30.1490.20. 2 hits.
    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. "Isolation, sequence and characterization of the maltose-regulated mlrA gene from the hyperthermophilic archaeum Pyrococcus furiosus."
      Robinson K.A., Schreier H.J.
      Gene 151:173-176(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    2. "Cloning and sequencing of a gene from the archaeon Pyrococcus furiosus with high homology to a gene encoding phosphoenolpyruvate synthetase from Escherichia coli."
      Jones C.E., Fleming T.M., Piper P.W., Littlechild J.A., Cowan D.A.
      Gene 160:101-103(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    3. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
      Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
      Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    4. "Phosphoenolpyruvate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus."
      Hutchins A.M., Holden J.F., Adams M.W.W.
      J. Bacteriol. 183:709-715(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiPPSA_PYRFU
    AccessioniPrimary (citable) accession number: P42850
    Secondary accession number(s): Q59672
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: April 3, 2002
    Last modified: January 20, 2016
    This is version 111 of the entry and version 3 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. 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.