A0A0J9BC22 · A0A0J9BC22_9GAMM

Function

function

Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Activity regulation

Activity of this regulatory enzyme is affected by several metabolites. Allosterically and non-competitively inhibited by fructose 1,6-bisphosphate (FBP) and unphosphorylated phosphocarrier protein EIIA-Glc (III-Glc), an integral component of the bacterial phosphotransferase (PTS) system.

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 site16ADP (UniProtKB | ChEBI)
Binding site16ATP (UniProtKB | ChEBI)
Binding site16sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site17ATP (UniProtKB | ChEBI)
Binding site18ATP (UniProtKB | ChEBI)
Binding site20ADP (UniProtKB | ChEBI)
Binding site86glycerol (UniProtKB | ChEBI)
Binding site86sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site87glycerol (UniProtKB | ChEBI)
Binding site87sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site138glycerol (UniProtKB | ChEBI)
Binding site138sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site237beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric inhibitor
Binding site239beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric inhibitor
Binding site248glycerol (UniProtKB | ChEBI)
Binding site248sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site249glycerol (UniProtKB | ChEBI)
Binding site270ADP (UniProtKB | ChEBI)
Binding site270ATP (UniProtKB | ChEBI)
Binding site313ADP (UniProtKB | ChEBI)
Binding site313ATP (UniProtKB | ChEBI)
Binding site317ATP (UniProtKB | ChEBI)
Binding site414ADP (UniProtKB | ChEBI)
Binding site414ATP (UniProtKB | ChEBI)
Binding site418ADP (UniProtKB | ChEBI)
Binding site481Zn2+ (UniProtKB | ChEBI); ligand shared with EIIA-Glc

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular Functionglycerol kinase activity
Molecular Functionmetal ion binding
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
      AI29_10410

Organism names

Accessions

  • Primary accession
    A0A0J9BC22

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer and homodimer (in equilibrium). Heterodimer with EIIA-Glc. Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain8-255Carbohydrate kinase FGGY N-terminal
Domain265-453Carbohydrate kinase FGGY C-terminal

Sequence similarities

Belongs to the FGGY kinase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    503
  • Mass (Da)
    55,973
  • Last updated
    2015-10-14 v1
  • Checksum
    46F0B5EF610CF32F
MSIKEKKYIVALDQGTTSSRAVILDHDANIVAVSQREFEQIYPKTGWVEHDPMDIWATQSSTLVEVLAHADISSDEVAAIGITNQRETTIVWDKETGKPIYNAIVWQDPRTADYCSGLKDQGYEDYIRDTTGLVINPYFSGTKVKWILDHVEGSRERAKRGELLFGTVDTWLVWKMTQGRVHITDYTNASRTMLFNIHTLEWDQKMLDLLDIPREILPEVKASSEVYGQTNIGGKGGTRIPIAGIAGDQQAALYGQLCVQPGMAKNTYGTGCFMLMNTGKEAITSKNGLLTTIACGPRGEVNYALEGAVFIGGASIQWLRDELKLFNDADDSEYFANKVKDSNGVYMVPAFTGLGAPYWDPYARGAIFGLTRGANANHIIRATLESIAFQTRDVLEAMQHDANTRLQTLRVDGGAVANNFLMQFQADILGAHVERPEVKEVTALGAAYLAGLAVGFWNDLEEVRSKSVVEKEFRPSIETTERNYRYAGWKKAVSRVRGWEKEE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JMSP01000321
EMBL· GenBank· DDBJ
KMV70714.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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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