Q98Q02 · KAD_MYCPU
- ProteinAdenylate kinase
- Geneadk
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids214 (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 | 12-17 | ATP (UniProtKB | ChEBI) | |||
Binding site | 33 | AMP (UniProtKB | ChEBI) | |||
Binding site | 38 | AMP (UniProtKB | ChEBI) | |||
Binding site | 59-61 | AMP (UniProtKB | ChEBI) | |||
Binding site | 88-91 | AMP (UniProtKB | ChEBI) | |||
Binding site | 95 | AMP (UniProtKB | ChEBI) | |||
Binding site | 127 | ATP (UniProtKB | ChEBI) | |||
Binding site | 130 | Zn2+ (UniProtKB | ChEBI); structural | |||
Binding site | 133 | Zn2+ (UniProtKB | ChEBI); structural | |||
Binding site | 150 | Zn2+ (UniProtKB | ChEBI); structural | |||
Binding site | 153 | Zn2+ (UniProtKB | ChEBI); structural | |||
Binding site | 160 | AMP (UniProtKB | ChEBI) | |||
Binding site | 171 | AMP (UniProtKB | ChEBI) | |||
Binding site | 199 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | intracellular membrane-bounded organelle | |
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
- Strain
- Taxonomic lineageBacteria > Mycoplasmatota > Mycoplasmoidales > Metamycoplasmataceae > Mycoplasmopsis
Accessions
- Primary accessionQ98Q02
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000158805 | 1-214 | Adenylate kinase | ||
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 32-61 | NMP | |||
Region | 126-163 | LID | |||
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.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length214
- Mass (Da)24,564
- Last updated2001-10-01 v1
- MD5 Checksum8E6D27AEC3B6373C0AA79D6F8393BA52
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL445565 EMBL· GenBank· DDBJ | CAC13740.1 EMBL· GenBank· DDBJ | Genomic DNA |