A0A1U7M093 · A0A1U7M093_9FIRM

Function

function

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

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site11ADP (UniProtKB | ChEBI)
Binding site11ATP (UniProtKB | ChEBI)
Binding site11sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site12ATP (UniProtKB | ChEBI)
Binding site13ATP (UniProtKB | ChEBI)
Binding site15ADP (UniProtKB | ChEBI)
Binding site81glycerol (UniProtKB | ChEBI)
Binding site81sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site82glycerol (UniProtKB | ChEBI)
Binding site82sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site133glycerol (UniProtKB | ChEBI)
Binding site133sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site242glycerol (UniProtKB | ChEBI)
Binding site242sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site243glycerol (UniProtKB | ChEBI)
Binding site264ADP (UniProtKB | ChEBI)
Binding site264ATP (UniProtKB | ChEBI)
Binding site307ADP (UniProtKB | ChEBI)
Binding site307ATP (UniProtKB | ChEBI)
Binding site408ADP (UniProtKB | ChEBI)
Binding site408ATP (UniProtKB | ChEBI)
Binding site412ADP (UniProtKB | ChEBI)

GO annotations

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

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
      BIV18_05965
      , HKO22_10010

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • 35-6-1
    • AGMB00490
  • Taxonomic lineage
    Bacteria > Bacillota > Tissierellia > Tissierellales > Peptoniphilaceae > Peptoniphilus

Accessions

  • Primary accession
    A0A1U7M093
  • Secondary accessions
    • A0A848RPI3

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer and homodimer (in equilibrium).

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-249Carbohydrate kinase FGGY N-terminal
Domain259-447Carbohydrate kinase FGGY C-terminal

Sequence similarities

Belongs to the FGGY kinase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    495
  • Mass (Da)
    55,838
  • Last updated
    2017-05-10 v1
  • Checksum
    EC24CE1780D7AF2F
MKYIMAFDAGTTSARTIIFDKKGNPVSVAQKELIKHFPKPGYVEEEPEDLWSKQIGTAVEAMSKKGIDPKDIAAIGITNQRETTIVWNKKTMEPVYNAIVWQCKRTTKYCEELKERGLEEKIKQKTGLVIDPYFSATKIRWILENVEGAREMANRGELLFGTVETYLIYKLTDGEVHITDYTNASRTMLFNIKEKRWDDELLEIFDIPRSMLPEIKNSSEVYGNSKSKYLGCEIPIASAIGDQQSSLFGTASFEKGMAKSTYGTGAFILMNTGDELIRSQNGLVSTIAWSINGKVKYALEGSIFEAGSCINFLRDNLRIIDQADDSEYMASKVKDTNDCYFIPAFTGLGAPYWDQYARGSIIGLTGSVNKYHIIRAALESIAYLSCDVVEAMQEDSMTKIKSLKVDGGVSKNNFLMQFLSDIVGVEVIRPKVIELTALGACYMAGLAVGFWKNIDEIRENNETEKCFEPKMKEEDRSKKMSRWHEAIKYSMNWAK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABDSR010000020
EMBL· GenBank· DDBJ
NMW86054.1
EMBL· GenBank· DDBJ
Genomic DNA
MJIH01000001
EMBL· GenBank· DDBJ
OLR65091.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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