P77439 · PTFX1_ECOLI

Function

function

Multifunctional protein that includes general (non sugar-specific) and sugar-specific components 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. The enzyme II FryABC PTS system is involved in fructose transport.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site15Pros-phosphohistidine intermediate; for HPr activity
Active site298Tele-phosphohistidine intermediate; for PTS EI activity
Binding site405phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site441phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site540Mg2+ (UniProtKB | ChEBI)
Binding site563-564phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site564Mg2+ (UniProtKB | ChEBI)
Binding site574phosphoenolpyruvate (UniProtKB | ChEBI)
Active site611Proton donor; for EI activity
Active site747Tele-phosphohistidine intermediate; for PTS EIIA activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentmembrane
Molecular Functionkinase activity
Molecular Functionmetal ion binding
Molecular Functionphosphoenolpyruvate-protein phosphotransferase activity
Molecular Functionprotein-N(PI)-phosphohistidine-sugar phosphotransferase activity
Biological Processphosphoenolpyruvate-dependent sugar phosphotransferase system

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Multiphosphoryl transfer protein 1
  • Short names
    MTP 1
  • Alternative names
    • Triphosphoryl transfer protein 1
      (TTP 1
      )

Including 3 domains:

  • Recommended name
    Phosphoenolpyruvate-protein phosphotransferase
  • EC number
  • Alternative names
    • Phosphotransferase system enzyme I
  • Recommended name
    Phosphocarrier protein HPr
  • Short names
    Protein H
  • Recommended name
    PTS system fructose-like EIIA component
  • EC number
  • Alternative names
    • Fructose-like phosphotransferase enzyme IIA component

Gene names

    • Name
      fryA
    • Synonyms
      ypdD
    • Ordered locus names
      b2383, JW2380

Organism names

  • Taxonomic identifier
  • Strains
    • K12 / W3110 / ATCC 27325 / DSM 5911
    • K12 / MG1655 / ATCC 47076
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P77439

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001470971-831Multiphosphoryl transfer protein 1
Modified residue15Phosphohistidine; by EI
Modified residue298Phosphohistidine; by autocatalysis
Modified residue747Phosphohistidine; by HPr

Keywords

Proteomic databases

Interaction

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P77439aceE P0AFG82EBI-545399, EBI-542683

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain1-90HPr
Region119-650PTS EI
Domain685-828PTS EIIA type-2

Domain

The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-2 domain.
In contrast to classical PTS systems, the fructose-like PTS has no requirement for HPr and Enzyme I; FryA combines a IIA domain with an Enzyme I and a HPr domains.

Sequence similarities

Belongs to the PEP-utilizing enzyme family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    831
  • Mass (Da)
    92,130
  • Last updated
    1997-02-01 v1
  • Checksum
    B9F3E3B6D4EAB597
MLTIQFLCPLPNGLHARPAWELKEQCSQWQSEITFINHRQNAKADAKSSLALIGTGTLFNDSCSLNISGSDEEQARRVLEEYIQVRFIDSDSVQPTQAELTAHPLPRSLSRLNPDLLYGNVLASGVGVGTLTLLQSDSLDSYRAIPASAQDSTRLEHSLATLAEQLNQQLRERDGESKTILSAHLSLIQDDEFAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDIRDISEQLLHITWPELKPRNKLVLEKPTILVAEDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPLDAIARYAGQPAVLDAQCGVLAINPNDAVSGYYQVAQTLADKRQKQQAQAAAQLAYSRDNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQQVLLAAGDKPIIFRTMDIGGDKSIPYLNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQILWVKGEIQKAIVELKRDGLRHAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPITPSFLRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDSEACRELARQACECRSAQEIEALLTAFTPEEDVRPLLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAKPIGWQSEMGEVELVIMLTLGANEGMNHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLLETELTF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U00096
EMBL· GenBank· DDBJ
AAC75442.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAA16253.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp