Q03DS8 · GLPK_PEDPA

Function

function

Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.

Catalytic activity

Activity regulation

Activated by phosphorylation and inhibited by fructose 1,6-bisphosphate (FBP).

Pathway

Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site13ADP (UniProtKB | ChEBI)
Binding site13ATP (UniProtKB | ChEBI)
Binding site13sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site14ATP (UniProtKB | ChEBI)
Binding site15ATP (UniProtKB | ChEBI)
Binding site17ADP (UniProtKB | ChEBI)
Binding site83glycerol (UniProtKB | ChEBI)
Binding site83sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site84glycerol (UniProtKB | ChEBI)
Binding site84sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site135glycerol (UniProtKB | ChEBI)
Binding site135sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site245glycerol (UniProtKB | ChEBI)
Binding site245sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site246glycerol (UniProtKB | ChEBI)
Binding site267ADP (UniProtKB | ChEBI)
Binding site267ATP (UniProtKB | ChEBI)
Binding site310ADP (UniProtKB | ChEBI)
Binding site310ATP (UniProtKB | ChEBI)
Binding site314ATP (UniProtKB | ChEBI)
Binding site411ADP (UniProtKB | ChEBI)
Binding site411ATP (UniProtKB | ChEBI)
Binding site415ADP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functionglycerol kinase activity
Biological Processglycerol catabolic process
Biological Processglycerol metabolic process
Biological Processglycerol-3-phosphate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glycerol kinase
  • EC number
  • Alternative names
    • ATP:glycerol 3-phosphotransferase
    • Glycerokinase
      (GK
      )

Gene names

    • Name
      glpK
    • Ordered locus names
      PEPE_1623

Organism names

Accessions

  • Primary accession
    Q03DS8

Proteomes

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_10000207551-504Glycerol kinase
Modified residue231Phosphohistidine; by HPr

Post-translational modification

The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), including enzyme I, and histidine-containing protein (HPr) are required for the phosphorylation, which leads to the activation of the enzyme.

Keywords

Interaction

Subunit

Homotetramer and homodimer (in equilibrium).

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the FGGY kinase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    504
  • Mass (Da)
    55,949
  • Last updated
    2006-11-14 v1
  • Checksum
    5C8B8024DA2F4931
MADKYILAIDEGTTSTRTIIFDHAGNKMADAQREFPQYFPKPGWVEHNANEIWNAVLSTIANAFIESGIKPNQISGIGITNQRETTVIWDKKTGLPIYNAVVWQSRQTAEIAEQLVKDGYGDMIHQKTGLVTDAYFSATKIRWILDHVDGAQARAERGELLFGTIDTWLMWKLTDGDVHVTDYSNASRTMLYNIHKLEWDKEILALLNIPASMLPEVKPNSTIYGKTKDYHFYGSEVPISGMAGDQQAALFGQLAFEPGMVKNTYGTGAFTVMNTGEKPQLSDNNLLTTIGYGINGKVYYALEGSIFVAGSAIQWLRDGMKLFKKASESEAAAVASQNDNEVYVVPAFTGLGAPYWDPNARGSVFGITRGTTREDFIKATLQSLAYQSRDVIDTMKKDSGIDIPSIRVDGGASNNDYLMQFQSDILGIEIDRASDLETTALGAAFLAGLAVGFWKDLEDLKKEYKPGKVFKPKMSTDEREDLYTGWQEAVAATRQFKHRPRQSK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000422
EMBL· GenBank· DDBJ
ABJ68644.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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