G7SPP0 · G7SPP0_9FLAO

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

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.

149650100150200250300350400450
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

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
      MADAR_183

Organism names

Accessions

  • Primary accession
    G7SPP0

Proteomes

Subcellular Location

Interaction

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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    496
  • Mass (Da)
    55,051
  • Last updated
    2012-01-25 v1
  • Checksum
    43EFB5006A00121C
MKKYVLSLDQGTTSSRAIIFDKIGNIISVAQREFTQIYPYPGWVEHNAEEIWSTQASVALEAILKANLEGENIVSIGITNQRETTVVWDKRTGEPIFNAIVWQDRRTSNYCDQIKYDGLTEMIRKKTGLVIDPYFSATKIKWILENVPGARDKANSGNLAFGTIDSWLIWNLTGKEIHVTDVTNASRTMLFNIHTLSWDQDLINLFDIPYTMLPSVKSSSEIFGYTTGHILSHKIPISGIAGDQQAALFGQMCTKIGMVKNTYGTGCFMLMNVGETPVFSQNNLITTIAWKIKDKIQYALEGSVFIAGAVVQWLRDGLGLLLSSSEAELLASSVENTEGLYMVPAFSGLGAPYWDQKARGTIVGITRGTSSAHFVRAALESIAFQNMDVLKAMEADSGISIKELRVDGGATVNKLLMQFQSEILNVKVVKSKISELTAAGAAYLAGLAVNYWTGLEEIQENWKLEHIFEPKGMSSRLERIKGWKRAIKTTRSWSSK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP003000
EMBL· GenBank· DDBJ
AER40499.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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