Q1GLQ4 · Q1GLQ4_RUEST
- ProteinGlycerol kinase
- GeneglpK
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids494 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
- glycerol + ATP = sn-glycerol 3-phosphate + ADP + H+
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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 11 | ADP (UniProtKB | ChEBI) | |||
Binding site | 11 | ATP (UniProtKB | ChEBI) | |||
Binding site | 11 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 12 | ATP (UniProtKB | ChEBI) | |||
Binding site | 13 | ATP (UniProtKB | ChEBI) | |||
Binding site | 15 | ADP (UniProtKB | ChEBI) | |||
Binding site | 81 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 81 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 82 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 82 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 133 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 133 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 242 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 242 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 243 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 264 | ADP (UniProtKB | ChEBI) | |||
Binding site | 264 | ATP (UniProtKB | ChEBI) | |||
Binding site | 307 | ADP (UniProtKB | ChEBI) | |||
Binding site | 307 | ATP (UniProtKB | ChEBI) | |||
Binding site | 311 | ATP (UniProtKB | ChEBI) | |||
Binding site | 409 | ADP (UniProtKB | ChEBI) | |||
Binding site | 409 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | glycerol kinase activity | |
Biological Process | glycerol catabolic process | |
Biological Process | glycerol-3-phosphate metabolic process | |
Biological Process | phosphorylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlycerol kinase
- EC number
- Alternative names
Gene names
Encoded on
- Plasmid megaplasmid TM1040
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Roseobacteraceae > Ruegeria
Accessions
- Primary accessionQ1GLQ4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 3-249 | Carbohydrate kinase FGGY N-terminal | |||
Domain | 260-448 | Carbohydrate kinase FGGY C-terminal | |||
Sequence similarities
Belongs to the FGGY kinase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length494
- Mass (Da)53,318
- Last updated2006-06-27 v1
- MD5 Checksum529ADF604DF283A1C6C3ECC3BF167ED9
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000376 EMBL· GenBank· DDBJ | ABF62412.1 EMBL· GenBank· DDBJ | Genomic DNA |