Q02YH8 · Q02YH8_LACLS

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.

150550100150200250300350400450500
TypeIDPosition(s)Description
Binding site21ADP (UniProtKB | ChEBI)
Binding site21ATP (UniProtKB | ChEBI)
Binding site21sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site22ATP (UniProtKB | ChEBI)
Binding site23ATP (UniProtKB | ChEBI)
Binding site25ADP (UniProtKB | ChEBI)
Binding site91glycerol (UniProtKB | ChEBI)
Binding site91sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site92glycerol (UniProtKB | ChEBI)
Binding site92sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site143glycerol (UniProtKB | ChEBI)
Binding site143sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site253glycerol (UniProtKB | ChEBI)
Binding site253sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site254glycerol (UniProtKB | ChEBI)
Binding site275ADP (UniProtKB | ChEBI)
Binding site275ATP (UniProtKB | ChEBI)
Binding site318ADP (UniProtKB | ChEBI)
Binding site318ATP (UniProtKB | ChEBI)
Binding site322ATP (UniProtKB | ChEBI)
Binding site419ADP (UniProtKB | ChEBI)
Binding site419ATP (UniProtKB | ChEBI)
Binding site423ADP (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
    • Ordered locus names
      LACR_1485

Organism names

Accessions

  • Primary accession
    Q02YH8

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue239Phosphohistidine; 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).

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain13-260Carbohydrate kinase FGGY N-terminal
Domain270-458Carbohydrate kinase FGGY C-terminal

Sequence similarities

Belongs to the FGGY kinase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    505
  • Mass (Da)
    55,678
  • Last updated
    2006-11-14 v1
  • Checksum
    70F4DFC79F5314A2
MSEGLPLEATEKYIMAIDQGTTSSRAIIFDHDGKHVGTSQKEFTQYFPEAGWVEHDANEIWNSVQSVIAGAFIESGIKPDQIAGIGITNQRETTVVWDKTTGLPIYHAIVWQSRQSASIADDLKNAGHAELFHKKTGLIIDSYFSATKIRWILDHVEGAQERAEKGELLFGTIDSWLVYKLTDGKVHVTDYSNASRTMLFNINTLEWDQEILDLLNIPKIMLPKAVSNSEVYGLTKTYHFFGSKVPIAGMAGDQQAALFGQMAFEPGMVKNTYGTGSFIVMNTGDKPQLSHNNLLTTIGYGINGEINYALEGSVFVAGSSIQWLRDGLKIIEKASDSEAAALESKNEDEIYMVPAFVGLGAPYWDQDARGAIFGLTRGTTDKDLIKATLQGIAYQVRDILGAMGEDTGIKIPILKVDGGATNNEYLMQFQADILNTSVQRAGDLETTALGAAFLAGLAVGYWKDFDELKESAKEGKRFDVQMEEERRNKLYSGWKKAVEATRSFE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000425
EMBL· GenBank· DDBJ
ABJ72994.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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