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Protein

Phosphoenolpyruvate-protein phosphotransferase

Gene

ptsI

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

Functioni

General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr) (PubMed:7876255, PubMed:12705838, PubMed:17053069). Can also use (Z)-3-fluoro-PEP (ZFPEP), (Z)-3-methyl-PEP (ZMePEP), (Z)-3-chloro-PEP (ZClPEP) and (E)-3-chloro-PEP (EClPEP) as alternative phosphoryl donors (PubMed:12705838).3 Publications

Catalytic activityi

Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.1 Publication

Cofactori

Mg2+1 Publication

Enzyme regulationi

Inhibited by oxalate.1 Publication

Kineticsi

Kcat is 3830 min(-1) with PEP as substrate. Kcat is 370 min(-1) with ZFPEP as substrate. Kcat is 285 min(-1) with ZMePEP as substrate. Kcat is 15.8 min(-1) with ZClPEP as substrate. Kcat is 2.8 min(-1) with EClPEP as substrate.1 Publication

Manual assertion based on experiment ini

  1. KM=0.11 mM for ZFPEP1 Publication
  2. KM=0.12 mM for EClPEP1 Publication
  3. KM=0.14 mM for PEP1 Publication
  4. KM=0.25 mM for ZClPEP1 Publication
  5. KM=0.43 mM for ZMePEP1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei189Tele-phosphohistidine intermediate2 Publications1
    Binding sitei296PEPBy similarity1
    Binding sitei332PEP1 Publication1
    Metal bindingi431Magnesium1 Publication1
    Metal bindingi455Magnesium1 Publication1
    Binding sitei465PEPBy similarity1
    Active sitei502Proton donor1 Publication1 Publication1

    GO - Molecular functioni

    • kinase activity Source: UniProtKB-KW
    • magnesium ion binding Source: EcoCyc
    • metal ion binding Source: EcoCyc
    • phosphoenolpyruvate-protein phosphotransferase activity Source: EcoCyc

    GO - Biological processi

    • phosphoenolpyruvate-dependent sugar phosphotransferase system Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Phosphotransferase system, Sugar transport, Transport

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PTSI-MONOMER.
    ECOL316407:JW2409-MONOMER.
    BRENDAi2.7.3.9. 2026.
    SABIO-RKP08839.

    Protein family/group databases

    TCDBi8.A.7.1.1. the phosphotransferase system enzyme i (ei) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoenolpyruvate-protein phosphotransferase1 Publication (EC:2.7.3.91 Publication)
    Alternative name(s):
    Phosphotransferase system, enzyme I1 Publication
    Gene namesi
    Name:ptsI1 Publication
    Ordered Locus Names:b2416, JW2409
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10789. ptsI.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • phosphoenolpyruvate-dependent sugar phosphotransferase complex Source: EcoCyc
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi189H → A: Very strong decrease of the affinity and catalytic efficiency for PEP. Inactive; when associated with A-502. 1 Publication1
    Mutagenesisi502C → A: Inactive; when associated with A-189. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001470671 – 575Phosphoenolpyruvate-protein phosphotransferaseAdd BLAST575

    Proteomic databases

    EPDiP08839.
    PaxDbiP08839.
    PRIDEiP08839.

    2D gel databases

    SWISS-2DPAGEP08839.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    bglGP119893EBI-551533,EBI-545674
    ptsHP0AA042EBI-551533,EBI-902853

    Protein-protein interaction databases

    BioGridi4260570. 498 interactors.
    851219. 1 interactor.
    DIPiDIP-10603N.
    IntActiP08839. 14 interactors.
    MINTiMINT-5290328.
    STRINGi511145.b2416.

    Structurei

    Secondary structure

    1575
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 8Combined sources4
    Beta strandi12 – 18Combined sources7
    Turni33 – 35Combined sources3
    Helixi36 – 65Combined sources30
    Helixi67 – 80Combined sources14
    Helixi83 – 96Combined sources14
    Helixi100 – 112Combined sources13
    Turni113 – 115Combined sources3
    Beta strandi116 – 118Combined sources3
    Helixi121 – 142Combined sources22
    Helixi149 – 151Combined sources3
    Beta strandi156 – 159Combined sources4
    Helixi165 – 170Combined sources6
    Helixi173 – 175Combined sources3
    Beta strandi176 – 180Combined sources5
    Beta strandi183 – 185Combined sources3
    Beta strandi186 – 188Combined sources3
    Helixi189 – 197Combined sources9
    Beta strandi201 – 203Combined sources3
    Helixi208 – 211Combined sources4
    Beta strandi217 – 220Combined sources4
    Turni222 – 225Combined sources4
    Beta strandi227 – 230Combined sources4
    Helixi233 – 239Combined sources7
    Turni240 – 243Combined sources4
    Helixi244 – 247Combined sources4
    Helixi254 – 256Combined sources3
    Beta strandi270 – 277Combined sources8
    Helixi279 – 286Combined sources8
    Beta strandi290 – 296Combined sources7
    Helixi297 – 301Combined sources5
    Beta strandi304 – 306Combined sources3
    Helixi310 – 323Combined sources14
    Turni324 – 326Combined sources3
    Beta strandi329 – 332Combined sources4
    Beta strandi337 – 339Combined sources3
    Helixi343 – 345Combined sources3
    Helixi353 – 355Combined sources3
    Helixi360 – 363Combined sources4
    Helixi367 – 380Combined sources14
    Beta strandi386 – 392Combined sources7
    Helixi396 – 415Combined sources20
    Beta strandi425 – 430Combined sources6
    Helixi433 – 437Combined sources5
    Helixi439 – 443Combined sources5
    Beta strandi447 – 451Combined sources5
    Helixi453 – 461Combined sources9
    Helixi468 – 473Combined sources6
    Beta strandi476 – 478Combined sources3
    Helixi479 – 494Combined sources16
    Beta strandi498 – 501Combined sources4
    Turni504 – 507Combined sources4
    Turni509 – 511Combined sources3
    Helixi512 – 517Combined sources6
    Beta strandi522 – 525Combined sources4
    Helixi527 – 529Combined sources3
    Helixi530 – 538Combined sources9
    Helixi542 – 554Combined sources13
    Helixi558 – 572Combined sources15

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1EZANMR-A1-258[»]
    1EZBNMR-A1-258[»]
    1EZCNMR-A1-258[»]
    1EZDNMR-A1-258[»]
    1ZYMX-ray2.50A/B1-258[»]
    2EZANMR-A1-258[»]
    2EZBNMR-A1-258[»]
    2EZCNMR-A1-258[»]
    2HWGX-ray2.70A/B1-575[»]
    2KX9Other-A/B1-573[»]
    2L5HOther-A/B1-573[»]
    2MP0NMR-A1-258[»]
    2N5TOther-A/B1-575[»]
    2XDFOther-A/B1-573[»]
    3EZANMR-A1-249[»]
    3EZBNMR-A1-258[»]
    3EZENMR-A1-258[»]
    ProteinModelPortaliP08839.
    SMRiP08839.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08839.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni454 – 455PEP binding1 Publication2

    Domaini

    The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.1 Publication

    Sequence similaritiesi

    Belongs to the PEP-utilizing enzyme family.Curated

    Phylogenomic databases

    eggNOGiENOG4105BZ3. Bacteria.
    COG1080. LUCA.
    HOGENOMiHOG000278513.
    InParanoidiP08839.
    KOiK08483.
    OMAiDYVLGFA.
    PhylomeDBiP08839.

    Family and domain databases

    Gene3Di1.10.274.10. 1 hit.
    3.20.20.60. 1 hit.
    3.50.30.10. 1 hit.
    InterProiIPR008279. PEP-util_enz_mobile_dom.
    IPR018274. PEP_util_AS.
    IPR000121. PEP_util_C.
    IPR023151. PEP_util_CS.
    IPR024692. PTS_EI.
    IPR006318. PTS_EI-like.
    IPR008731. PTS_EIN.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view]
    PfamiPF05524. PEP-utilisers_N. 1 hit.
    PF00391. PEP-utilizers. 1 hit.
    PF02896. PEP-utilizers_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000732. PTS_enzyme_I. 1 hit.
    SUPFAMiSSF47831. SSF47831. 1 hit.
    SSF51621. SSF51621. 1 hit.
    SSF52009. SSF52009. 1 hit.
    TIGRFAMsiTIGR01417. PTS_I_fam. 1 hit.
    PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
    PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P08839-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MISGILASPG IAFGKALLLK EDEIVIDRKK ISADQVDQEV ERFLSGRAKA
    60 70 80 90 100
    SAQLETIKTK AGETFGEEKE AIFEGHIMLL EDEELEQEII ALIKDKHMTA
    110 120 130 140 150
    DAAAHEVIEG QASALEELDD EYLKERAADV RDIGKRLLRN ILGLKIIDLS
    160 170 180 190 200
    AIQDEVILVA ADLTPSETAQ LNLKKVLGFI TDAGGRTSHT SIMARSLELP
    210 220 230 240 250
    AIVGTGSVTS QVKNDDYLIL DAVNNQVYVN PTNEVIDKMR AVQEQVASEK
    260 270 280 290 300
    AELAKLKDLP AITLDGHQVE VCANIGTVRD VEGAERNGAE GVGLYRTEFL
    310 320 330 340 350
    FMDRDALPTE EEQFAAYKAV AEACGSQAVI VRTMDIGGDK ELPYMNFPKE
    360 370 380 390 400
    ENPFLGWRAI RIAMDRREIL RDQLRAILRA SAFGKLRIMF PMIISVEEVR
    410 420 430 440 450
    ALRKEIEIYK QELRDEGKAF DESIEIGVMV ETPAAATIAR HLAKEVDFFS
    460 470 480 490 500
    IGTNDLTQYT LAVDRGNDMI SHLYQPMSPS VLNLIKQVID ASHAEGKWTG
    510 520 530 540 550
    MCGELAGDER ATLLLLGMGL DEFSMSAISI PRIKKIIRNT NFEDAKVLAE
    560 570
    QALAQPTTDE LMTLVNKFIE EKTIC
    Length:575
    Mass (Da):63,562
    Last modified:November 1, 1988 - v1
    Checksum:i4278F0838855E950
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J02796 Genomic DNA. Translation: AAA24441.1.
    M10425 Genomic DNA. Translation: AAA24439.1.
    U00096 Genomic DNA. Translation: AAC75469.1.
    AP009048 Genomic DNA. Translation: BAA16290.1.
    M21994 Genomic DNA. Translation: AAA24385.1.
    M21451 Genomic DNA. Translation: AAA23656.1.
    PIRiB29785. WQECPI.
    RefSeqiNP_416911.1. NC_000913.3.
    WP_000623140.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75469; AAC75469; b2416.
    BAA16290; BAA16290; BAA16290.
    GeneIDi946879.
    KEGGiecj:JW2409.
    eco:b2416.
    PATRICi32120215. VBIEscCol129921_2510.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J02796 Genomic DNA. Translation: AAA24441.1.
    M10425 Genomic DNA. Translation: AAA24439.1.
    U00096 Genomic DNA. Translation: AAC75469.1.
    AP009048 Genomic DNA. Translation: BAA16290.1.
    M21994 Genomic DNA. Translation: AAA24385.1.
    M21451 Genomic DNA. Translation: AAA23656.1.
    PIRiB29785. WQECPI.
    RefSeqiNP_416911.1. NC_000913.3.
    WP_000623140.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1EZANMR-A1-258[»]
    1EZBNMR-A1-258[»]
    1EZCNMR-A1-258[»]
    1EZDNMR-A1-258[»]
    1ZYMX-ray2.50A/B1-258[»]
    2EZANMR-A1-258[»]
    2EZBNMR-A1-258[»]
    2EZCNMR-A1-258[»]
    2HWGX-ray2.70A/B1-575[»]
    2KX9Other-A/B1-573[»]
    2L5HOther-A/B1-573[»]
    2MP0NMR-A1-258[»]
    2N5TOther-A/B1-575[»]
    2XDFOther-A/B1-573[»]
    3EZANMR-A1-249[»]
    3EZBNMR-A1-258[»]
    3EZENMR-A1-258[»]
    ProteinModelPortaliP08839.
    SMRiP08839.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260570. 498 interactors.
    851219. 1 interactor.
    DIPiDIP-10603N.
    IntActiP08839. 14 interactors.
    MINTiMINT-5290328.
    STRINGi511145.b2416.

    Protein family/group databases

    TCDBi8.A.7.1.1. the phosphotransferase system enzyme i (ei) family.

    2D gel databases

    SWISS-2DPAGEP08839.

    Proteomic databases

    EPDiP08839.
    PaxDbiP08839.
    PRIDEiP08839.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75469; AAC75469; b2416.
    BAA16290; BAA16290; BAA16290.
    GeneIDi946879.
    KEGGiecj:JW2409.
    eco:b2416.
    PATRICi32120215. VBIEscCol129921_2510.

    Organism-specific databases

    EchoBASEiEB0782.
    EcoGeneiEG10789. ptsI.

    Phylogenomic databases

    eggNOGiENOG4105BZ3. Bacteria.
    COG1080. LUCA.
    HOGENOMiHOG000278513.
    InParanoidiP08839.
    KOiK08483.
    OMAiDYVLGFA.
    PhylomeDBiP08839.

    Enzyme and pathway databases

    BioCyciEcoCyc:PTSI-MONOMER.
    ECOL316407:JW2409-MONOMER.
    BRENDAi2.7.3.9. 2026.
    SABIO-RKP08839.

    Miscellaneous databases

    EvolutionaryTraceiP08839.
    PROiP08839.

    Family and domain databases

    Gene3Di1.10.274.10. 1 hit.
    3.20.20.60. 1 hit.
    3.50.30.10. 1 hit.
    InterProiIPR008279. PEP-util_enz_mobile_dom.
    IPR018274. PEP_util_AS.
    IPR000121. PEP_util_C.
    IPR023151. PEP_util_CS.
    IPR024692. PTS_EI.
    IPR006318. PTS_EI-like.
    IPR008731. PTS_EIN.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view]
    PfamiPF05524. PEP-utilisers_N. 1 hit.
    PF00391. PEP-utilizers. 1 hit.
    PF02896. PEP-utilizers_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000732. PTS_enzyme_I. 1 hit.
    SUPFAMiSSF47831. SSF47831. 1 hit.
    SSF51621. SSF51621. 1 hit.
    SSF52009. SSF52009. 1 hit.
    TIGRFAMsiTIGR01417. PTS_I_fam. 1 hit.
    PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
    PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPT1_ECOLI
    AccessioniPrimary (citable) accession number: P08839
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1988
    Last modified: November 2, 2016
    This is version 173 of the entry and version 1 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.1 Publication
    Enzyme I of the sugar PTS has been shown to phosphorylate NPr of the nitrogen-metabolic PTS, though much less efficiently than it does HPr. This process may link carbon and nitrogen assimilation.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    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.