A0A210VWS8 · A0A210VWS8_9BURK

  • Protein
    HPr kinase/phosphorylase
  • Gene
    hprK
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr).

Miscellaneous

Both phosphorylation and phosphorolysis are carried out by the same active site and suggest a common mechanism for both reactions.

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 site146
Binding site161-168ATP (UniProtKB | ChEBI)
Active site167
Binding site168Mg2+ (UniProtKB | ChEBI)
Active site185Proton acceptor; for phosphorylation activity. Proton donor; for dephosphorylation activity
Binding site210Mg2+ (UniProtKB | ChEBI)
Active site252

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular Functionphosphorelay sensor kinase activity
Molecular Functionprotein serine/threonine kinase activity
Molecular Functionprotein serine/threonine/tyrosine kinase activity
Biological Processregulation of carbohydrate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    HPr kinase/phosphorylase
  • EC number
  • Short names
    HPrK/P
  • Alternative names
    • HPr(Ser) kinase/phosphorylase

Gene names

    • Name
      hprK
    • ORF names
      KDK82_3704

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • K82
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Comamonadaceae > Delftia

Accessions

  • Primary accession
    A0A210VWS8

Proteomes

Interaction

Subunit

Homohexamer.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain11-135HPr(Ser) kinase/phosphorylase N-terminal
Domain138-307HPr kinase/phosphorylase C-terminal
Region209-218Important for the catalytic mechanism of both phosphorylation and dephosphorylation
Region273-278Important for the catalytic mechanism of dephosphorylation

Domain

The Walker A ATP-binding motif also binds Pi and PPi.

Sequence similarities

Belongs to the HPrK/P family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    318
  • Mass (Da)
    35,725
  • Last updated
    2017-11-22 v1
  • Checksum
    8203286873619C91
MRPSAISADVLFEEFRSSLRWEWVAGLGASERRFDEMAVRSARSGADLVGYLNYIHPYRLQVLGEREIAYLSNATPQDCQRRVARIVTLEPPVLVLADGQTAPDALLSMCERAHIPMFSTREQSAFVIDVLRAYLAKHFADRTTMHGVFMDILGMGVLITGESGLGKSELGLELVTRGNGLVADDAVDLYRINQTTIEGKCPELLQNLLEVRGIGLLDIRAIFGETAVRRKMRLKLIVHLVRKETMEREYERLPAEPLTQDVLGVPVRKVVIQVVAGRNIAVLVEAAVRNAILQLRGIDTYQEFVQRHRRAMERGDTF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MYFL01000003
EMBL· GenBank· DDBJ
OWG14458.1
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