A0A1C7WEC9 · A0A1C7WEC9_9GAMM

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

Function

function

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

Caution

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

Catalytic activity

Activity regulation

Activity of this regulatory enzyme is affected by several metabolites. Allosterically and non-competitively inhibited by fructose 1,6-bisphosphate (FBP) and unphosphorylated phosphocarrier protein EIIA-Glc (III-Glc), an integral component of the bacterial phosphotransferase (PTS) system.

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 site15ADP (UniProtKB | ChEBI)
Binding site15ATP (UniProtKB | ChEBI)
Binding site15sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site16ATP (UniProtKB | ChEBI)
Binding site17ATP (UniProtKB | ChEBI)
Binding site19ADP (UniProtKB | ChEBI)
Binding site85glycerol (UniProtKB | ChEBI)
Binding site85sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site86glycerol (UniProtKB | ChEBI)
Binding site86sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site137glycerol (UniProtKB | ChEBI)
Binding site137sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site236beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric inhibitor
Binding site238beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric inhibitor
Binding site247glycerol (UniProtKB | ChEBI)
Binding site247sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site248glycerol (UniProtKB | ChEBI)
Binding site269ADP (UniProtKB | ChEBI)
Binding site269ATP (UniProtKB | ChEBI)
Binding site312ADP (UniProtKB | ChEBI)
Binding site312ATP (UniProtKB | ChEBI)
Binding site316ATP (UniProtKB | ChEBI)
Binding site413ADP (UniProtKB | ChEBI)
Binding site413ATP (UniProtKB | ChEBI)
Binding site417ADP (UniProtKB | ChEBI)
Binding site480Zn2+ (UniProtKB | ChEBI); ligand shared with EIIA-Glc

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular Functionglycerol kinase activity
Molecular Functionmetal ion binding
Biological Processglycerol catabolic 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
    • ORF names
      A6U95_20570

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 14-2641
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Yersiniaceae > Serratia

Accessions

  • Primary accession
    A0A1C7WEC9

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer and homodimer (in equilibrium). Heterodimer with EIIA-Glc. Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-254Carbohydrate kinase FGGY N-terminal
Domain264-452Carbohydrate kinase FGGY C-terminal

Sequence similarities

Belongs to the FGGY kinase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    502
  • Mass (Da)
    55,728
  • Last updated
    2016-11-30 v1
  • Checksum
    F8CD29D0644B632A
MTTEKKYIVALDQGTTSSRAVVLDHDANIVAVSQREFTQIYPKAGWVEHDPMEIWSSQSSTLVEVLAKADISSDQIAGIGITNQRETTIVWEKETGKPIYNAIVWQCRRTADICEKLKRDGLEEYIRHNTGLVVDPYFSGTKVKWILDHVEGARERAKRGELLFGTVDTWLVWKMTQGRVHVTDYTNASRTMMFNIHELDWDDRMLEALDIPRAMLPKVRPSSEVYGQTNIGGKGGTRIPIAGIAGDQQAALYGQLCVQPGMAKNTYGTGCFLLMNTGKEAVRSNHGLLTTIACGPRGEVNYALEGAVFIGGASIQWLRDELKLISDAADSEYFATKVKDSNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLDAMQADANTRLQSLRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAIGYWSDLDELKSKAAIEREFRPGIETTERNFRYSGWKKAVARAQAWEDHD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LXKR01000008
EMBL· GenBank· DDBJ
OCJ43477.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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