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A0A174I181 · A0A174I181_9FIRM

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.

149850100150200250300350400450
TypeIDPosition(s)Description
Binding site12ADP (UniProtKB | ChEBI)
Binding site12ATP (UniProtKB | ChEBI)
Binding site12sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site13ATP (UniProtKB | ChEBI)
Binding site14ATP (UniProtKB | ChEBI)
Binding site16ADP (UniProtKB | ChEBI)
Binding site82glycerol (UniProtKB | ChEBI)
Binding site82sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site83glycerol (UniProtKB | ChEBI)
Binding site83sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site134glycerol (UniProtKB | ChEBI)
Binding site134sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site243glycerol (UniProtKB | ChEBI)
Binding site243sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site244glycerol (UniProtKB | ChEBI)
Binding site265ADP (UniProtKB | ChEBI)
Binding site265ATP (UniProtKB | ChEBI)
Binding site308ADP (UniProtKB | ChEBI)
Binding site308ATP (UniProtKB | ChEBI)
Binding site312ATP (UniProtKB | ChEBI)
Binding site409ADP (UniProtKB | ChEBI)
Binding site409ATP (UniProtKB | ChEBI)
Binding site413ADP (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
      ERS852497_00857

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 2789STDY5834884
  • Taxonomic lineage
    Bacteria > Bacillota > Clostridia > Lachnospirales > Lachnospiraceae > Agathobacter

Accessions

  • Primary accession
    A0A174I181

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer and homodimer (in equilibrium).

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-250Carbohydrate kinase FGGY N-terminal
Domain260-448Carbohydrate kinase FGGY C-terminal

Sequence similarities

Belongs to the FGGY kinase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    498
  • Mass (Da)
    55,125
  • Last updated
    2016-09-07 v1
  • MD5 Checksum
    D054F2D39CE3F0F1D1124C0451FBF645
MAKYIMALDAGTTSNRCILFNEKGEMCSVAQKEFTQFFPKPGWVEHDAEEIWATQLEVAKEAMANIQATAADICAIGITNQRETTIVWDKNTGEPVYHAIVWQCRRTAEYADSLKEKGLTETFRKKTGLVIDAYFSATKLKWLLDNVPGARERAERGELLFGTVETWLIWKLTQGQVHVTDYSNASRTMMFNINTLKWDDEILKELDIPKSMLPKPMPSSCVYGEVNPVYFGGPIPIAGAAGDQQAALFGQTCFRAGEAKNTYGTGCFLLMNTGEMPVSSKNGLVTTIAWGIDGKVVYALEGSIFVAGASIQWLRDEMKFIDSSTDSEYMARKVKDTNGCYVVPAFTGLGAPYWDQYARGTIVGLTRGVNKYHVIRATLESMAFQVNDVLEAMKADSGINLTSLKVDGGASANNLLMQMQADISNAPVNRPVCVETTAMGAAYLAGLAVGYWDSMDDIKRNWSIDRVFEPEIAADLREKKLKMWKKAVACAFNWAKDD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CZAJ01000005
EMBL· GenBank· DDBJ
CUO79666.1
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.
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