A0A6A7Y4P2 · A0A6A7Y4P2_9HYPH
- ProteinGlycerol kinase
- GeneglpK
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids495 (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
- ATP + glycerol = ADP + H+ + sn-glycerol 3-phosphate
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) | ||||
Sequence: T | ||||||
Binding site | 11 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 11 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 12 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 13 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 15 | ADP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 81 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 81 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 82 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 82 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 133 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 133 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 242 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 242 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 243 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 264 | ADP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 264 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 307 | ADP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 307 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 311 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 410 | ADP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 410 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | glycerol kinase activity | |
Biological Process | glycerol catabolic process | |
Biological Process | glycerol-3-phosphate metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlycerol kinase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Segnochrobactraceae > Segnochrobactrum
Accessions
- Primary accessionA0A6A7Y4P2
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-249 | Carbohydrate kinase FGGY N-terminal | ||||
Sequence: ILAIDQGTTSSRAILFDAAMRLKAVAQQEFPQHFPASGWVEHDPADLWSSVAGTARAAIEQAGLTGADIAAIGITNQRETVVIWDRATGEPIHRAIVWQDRRTADLCARLKADGLEPEISAKTGLLIDPYFSATKIKWLLDHVEGARERARRGELAFGTVDCFLIWKLTDGAVHATDATNAARTMLYDIREGRWDEALCAAFGVPMAMLPEVRDCAAPYGTTRPDLFGRAIPILGVAGDQQAATVG | ||||||
Domain | 260-448 | Carbohydrate kinase FGGY C-terminal | ||||
Sequence: STYGTGCFALLNTGDDLVASKNRLLGTIAYRLKGRTTYALEGSIFIAGAVVQWLRDGLKIIRHAAETHPLAEKADPAQDLVLVPAFTGLGAPYWRPDCRGAVFGLTRNSGPAEFARAALESVGYQTRDLLEAMHADWKDATAEGVLRVDGGMTASDWTMQFLADILGAPVDRPVVRETTALGAAYLAGL |
Sequence similarities
Belongs to the FGGY kinase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length495
- Mass (Da)53,598
- Last updated2020-06-17 v1
- Checksum442EC35584C87030
Keywords
- Technical term