A0A0A1H2Q1 · A0A0A1H2Q1_9BURK
- ProteinAdenylate kinase
- Geneadk
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids216 (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 | 8-13 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GAGKGT | ||||||
Binding site | 29 | AMP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 34 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 55-57 | AMP (UniProtKB | ChEBI) | ||||
Sequence: QLV | ||||||
Binding site | 83-86 | AMP (UniProtKB | ChEBI) | ||||
Sequence: GFPR | ||||||
Binding site | 90 | AMP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 121 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 130-131 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SY | ||||||
Binding site | 154 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 165 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 201 | 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 | |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales
Accessions
- Primary accessionA0A0A1H2Q1
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 28-57 | NMP | ||||
Sequence: STGDMLRAAVKAGTPLGLAAKKVMEAGQLV | ||||||
Region | 120-157 | LID | ||||
Sequence: GRRVHPGSGRSYHVRFNPPKIADRDDHTGEPLVQRDDD | ||||||
Domain | 121-156 | Adenylate kinase active site lid | ||||
Sequence: RRVHPGSGRSYHVRFNPPKIADRDDHTGEPLVQRDD | ||||||
Region | 126-151 | Disordered | ||||
Sequence: GSGRSYHVRFNPPKIADRDDHTGEPL | ||||||
Compositional bias | 136-151 | Basic and acidic residues | ||||
Sequence: NPPKIADRDDHTGEPL |
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.
Sequence similarities
Belongs to the adenylate kinase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length216
- Mass (Da)23,592
- Last updated2015-02-04 v1
- ChecksumFEB4E06EBE9A1D6A
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 136-151 | Basic and acidic residues | ||||
Sequence: NPPKIADRDDHTGEPL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP014683 EMBL· GenBank· DDBJ | BAP88603.1 EMBL· GenBank· DDBJ | Genomic DNA |