C0QVC0 · GLPK_BRAHW

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.

149450100150200250300350400450
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 site241glycerol (UniProtKB | ChEBI)
Binding site241sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site242glycerol (UniProtKB | ChEBI)
Binding site263ADP (UniProtKB | ChEBI)
Binding site263ATP (UniProtKB | ChEBI)
Binding site306ADP (UniProtKB | ChEBI)
Binding site306ATP (UniProtKB | ChEBI)
Binding site310ATP (UniProtKB | ChEBI)
Binding site407ADP (UniProtKB | ChEBI)
Binding site407ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functionglycerol kinase activity
Biological Processglycerol catabolic process
Biological Processglycerol metabolic 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
      BHWA1_01960

Organism names

Accessions

  • Primary accession
    C0QVC0

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10001241831-494Glycerol kinase

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the FGGY kinase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    494
  • Mass (Da)
    55,087
  • Last updated
    2009-05-05 v1
  • Checksum
    83C377F6F95068A8
MAKYVVAIDQGTTSSRAIVFDYDQNMVSVAQKEFTQIYPHEGWVEHNAAEIWATQFGVLQEAIQIAGVKPEEIAAIGITNQRETTVVWDKNTGEPIYNAIVWQCRRTAPICDELKKKGLDTYIRENTGLVVDAYFSGTKIKWILDNVPGAREKANKGELLFGTIDTWLVWKLTGGKVHVTDYTNASRTMIYNIKELKWDETILKELDIPMSMLPEVKDSSCIYGYAHINGKEVPISGIAGDQQSALFGQAGFNKGDTKNTYGTGSFILMNIGENFILSKNGLITTIAIGYNGKIEYALEGSVFIAGAVIQWVRDELRLLHDAKDTEYFATKVKDTNGVYLVPAFVGLGAPYWDMYARGCLVGITRGVNRSHIIRAAEEAIAYQSKDVIDAMVADSGVKLSSLKVDGGACRDNFLMQFQSDIINTKVLRPQITETTALGAAYLAGLAVGFWKDKDEITNRWKLEREFTPSLSEEERNKKYMGWKKAVERSRGWAL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001357
EMBL· GenBank· DDBJ
ACN84421.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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