A0A1S2N0C5 · A0A1S2N0C5_9MICC

  • Protein
    Phosphoenolpyruvate-protein phosphotransferase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

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).

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site188Tele-phosphohistidine intermediate
Binding site288phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site324phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site413Mg2+ (UniProtKB | ChEBI)
Binding site436-437phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site437Mg2+ (UniProtKB | ChEBI)
Binding site447phosphoenolpyruvate (UniProtKB | ChEBI)
Active site490Proton donor

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionkinase activity
Molecular Functionmetal ion binding
Molecular Functionphosphoenolpyruvate-protein phosphotransferase activity
Biological Processphosphoenolpyruvate-dependent sugar phosphotransferase system
Biological Processphosphorylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphoenolpyruvate-protein phosphotransferase
  • EC number
  • Alternative names
    • Phosphotransferase system, enzyme I

Gene names

    • ORF names
      BK826_09385

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • LCT-H5
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micrococcales > Micrococcaceae > Rothia

Accessions

  • Primary accession
    A0A1S2N0C5

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain, coiled coil.

TypeIDPosition(s)Description
Domain5-125Phosphotransferase system enzyme I N-terminal
Coiled coil41-68
Domain154-223PEP-utilising enzyme mobile
Domain255-528PEP-utilising enzyme C-terminal

Sequence similarities

Belongs to the PEP-utilizing enzyme family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    565
  • Mass (Da)
    59,218
  • Last updated
    2017-04-12 v1
  • Checksum
    873F72E4397B9488
MDKLTGVGVSAGRVIGPVLQMPEPIREPDAASTLAEGESPEAAVERLKEAAEAVKENLKERAGRASGNAAAVLKSTALMAGDKALLKNAGKLVTDKGLSPERAIWEAAGDYAAQMKALGGYMAQRVTDILDVRSRIVAQLTGQPAPGIPESETEFVLVAEDLAPADTATLDPAKVIALVTSEGGPQAHTAILARDLGLPAIVAANGAREIPDGTTVYVDATDGTVVTTPGEKEYRLAEAYANRKPLPEFDGTGKLADGTEIPLYSNVGNGKAAQTAAEAKAEGIGLFRTEFAFLNRDEEPSVEEQTVEYKAVFDAFPGRHIVVRTLDAGADKPLPFLTDTSEPNPALGVRGYRTDWTSPGVLQRQIEAIAAAAKDSTADVWVMAPMISTAPEAHDFSAMLEEAGLKTHGVMVETPSAAVTSRDILHEVDFVSVGTNDLTQYTMAADRLLGPLAELNNPWQPGVLRMIDLTVRGARQAEDETGKAKSVSVCGEAAADPALAVVLVGLGVNALSMNTRSIPAVAAVLKSVTLEKAQQIAVQVLDARSAENAKDVARAELPVLDELGL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MODZ01000013
EMBL· GenBank· DDBJ
OIJ35011.1
EMBL· GenBank· DDBJ
Genomic DNA

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