Q24MZ3 · Q24MZ3_DESHY

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 site46ADP (UniProtKB | ChEBI)
Binding site46ATP (UniProtKB | ChEBI)
Binding site46sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site47ATP (UniProtKB | ChEBI)
Binding site48ATP (UniProtKB | ChEBI)
Binding site50ADP (UniProtKB | ChEBI)
Binding site116glycerol (UniProtKB | ChEBI)
Binding site116sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site117glycerol (UniProtKB | ChEBI)
Binding site117sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site168glycerol (UniProtKB | ChEBI)
Binding site168sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site278glycerol (UniProtKB | ChEBI)
Binding site278sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site279glycerol (UniProtKB | ChEBI)
Binding site300ADP (UniProtKB | ChEBI)
Binding site300ATP (UniProtKB | ChEBI)
Binding site343ADP (UniProtKB | ChEBI)
Binding site343ATP (UniProtKB | ChEBI)
Binding site347ATP (UniProtKB | ChEBI)
Binding site444ADP (UniProtKB | ChEBI)
Binding site444ATP (UniProtKB | ChEBI)
Binding site448ADP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functionglycerol kinase activity
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
    • Ordered locus names
      DSY4810

Organism names

Accessions

  • Primary accession
    Q24MZ3

Proteomes

Interaction

Subunit

Homotetramer and homodimer (in equilibrium).

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain38-285Carbohydrate kinase FGGY N-terminal
Domain295-483Carbohydrate kinase FGGY C-terminal

Sequence similarities

Belongs to the FGGY kinase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    528
  • Mass (Da)
    58,585
  • Last updated
    2006-04-18 v1
  • Checksum
    862E5C73E9A8955E
MTEGTAVVFCKTIEIPKDAKFKVKADAGRIRGKTMKKYVLALDQGTTSCRAILFDRESQIVGVAQKEFTQIYPQPGWVEHDPEEVWSTQYGVIAELLARYQVTSEEIAGIGITNQRETTVVWDKHTGKSVTNAIVWQCRRTAPLCDELKMKGLEPLFKEKTGLVLDAYFSGTKIRWILDRVPGAQEKAEKGELLFGTMDTWLVWNLTKGRIHVTDYSNASRTLLYNIKTLAWDPDLLQVLNIPLAMLPEVKPSSTIYGETAAEGLFGHPIPIAGIAGDQQAALFGQACFAPGMAKNTYGTGCFMLLNTGEELYESRHGLISTIAWGLDEKVIYALEGSVFMAGAVMQWLRDELKLIETAGDSEYFAGKVADNGGVYLVPAFTGLGAPYWDMDARGAIVGLTRGSNKNHIIRAALESMAYQTRDILEAMEADSQLPLQLLKVDGGAVVNNLLMQFQADILGVEVERPHCIETTALGAAYLAGLAIGFWSSKEELRDKAKMERSFKPQMAEERKEKYYQGWHKAVRQIME

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP008230
EMBL· GenBank· DDBJ
BAE86599.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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