A0A2T4RRM7 · A0A2T4RRM7_MAMSC

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.

149750100150200250300350400450
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
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
    • ORF names
      CEP64_06845
      , G6W75_00405
      , JCQ35_05115

Organism names

Accessions

  • Primary accession
    A0A2T4RRM7

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue229Phosphohistidine; 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).

Protein-protein interaction databases

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
    497
  • Mass (Da)
    55,745
  • Last updated
    2018-07-18 v1
  • Checksum
    86F570346A8DB72C
MEKYILSIDQGTTSSRAILFDKEGTIKFVSQREFKQYFPKGGWVEHDANEIWTSVLAVISSVLNENNISPKQIEGIGITNQRETAVVWDKNTGRPVYHAIVWQSRQTQDICTELKSKDLEPIFKEKTGLLLDPYFSGTKVKWILDNVEGAREKAENGDLLFGTIDTWLIWKFTGDVHVTDYSNASRTLMYNIYDLKWDEELLEYLDVPASMLPEVKPSSEVYGYTQEHHFFGEKIAIAGVAGDQQAALFGQACFESGEVKNTYGTGGFMLMNTGEKAVKSESGLLTTLAYGLDGKVNYALEGSIFVSGSAIQWLRDGLRMIKSAPASEDYANRVKSTEGVYVVPAFVGLGTPYWDADARGAIFGLTRGTEKEHFIRATLESLCYQTRDVLEAMEKDSGINVETLRVDGGAVKNNFLMQFQADIVNTPVERPEVNETTALGAAYLAGLAVGFWKSKDEIKQRWKLETEFKPELEEEEREKLYKGWKTAVKATQAFKLD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP022046
EMBL· GenBank· DDBJ
ASE34306.1
EMBL· GenBank· DDBJ
Genomic DNA
JAAMFH010000001
EMBL· GenBank· DDBJ
NGX74551.1
EMBL· GenBank· DDBJ
Genomic DNA
CP065960
EMBL· GenBank· DDBJ
QQC96409.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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