A0A1F5BCK9 · A0A1F5BCK9_9BACT
- ProteinAdenylate kinase
- Geneadk
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids223 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic activity
- AMP + ATP = 2 ADP
Pathway
Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 10-15 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GSGKGT | ||||||
Binding site | 31 | AMP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 36 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 57-59 | AMP (UniProtKB | ChEBI) | ||||
Sequence: GLV | ||||||
Binding site | 85-88 | AMP (UniProtKB | ChEBI) | ||||
Sequence: GFPR | ||||||
Binding site | 92 | AMP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 124 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 127 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: C | ||||||
Binding site | 130 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: C | ||||||
Binding site | 133-134 | ATP (UniProtKB | ChEBI) | ||||
Sequence: IY | ||||||
Binding site | 147 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: C | ||||||
Binding site | 150 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: C | ||||||
Binding site | 157 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 168 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 196 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | adenylate kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | nucleoside diphosphate kinase activity | |
Molecular Function | zinc ion binding | |
Biological Process | AMP salvage | |
Biological Process | nucleoside diphosphate metabolic process | |
Biological Process | phosphorylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenylate kinase
- EC number
- Short namesAK
- Alternative names
Gene names
Organism names
- Taxonomic lineageBacteria > Candidatus Aminicenantota
Accessions
- Primary accessionA0A1F5BCK9
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 30-59 | NMP | ||||
Sequence: STGDLLREAVREGTPLGIVAASQMGKGGLV | ||||||
Region | 123-160 | LID | ||||
Sequence: NRRTCPKCEAIYHLLNKPPKTAGICDACGTALVQRNDD | ||||||
Domain | 124-159 | Adenylate kinase active site lid | ||||
Sequence: RRTCPKCEAIYHLLNKPPKTAGICDACGTALVQRND |
Domain
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Sequence similarities
Belongs to the adenylate kinase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length223
- Mass (Da)23,560
- Last updated2017-02-15 v1
- ChecksumF1F7DAE42CF54479