A0A2H3DA29 · A0A2H3DA29_ARMGA
- ProteinAdenylate kinase
- GeneADK1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids255 (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. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.
Catalytic activity
- AMP + ATP = 2 ADP
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 48-53 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GAGKGT | ||||||
Binding site | 69 | AMP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 74 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 95-97 | AMP (UniProtKB | ChEBI) | ||||
Sequence: GLV | ||||||
Binding site | 124-127 | AMP (UniProtKB | ChEBI) | ||||
Sequence: GFPR | ||||||
Binding site | 131 | AMP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 166 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 175-176 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SY | ||||||
Binding site | 199 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 210 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 238 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrial intermembrane space | |
Molecular Function | adenylate kinase activity | |
Molecular Function | ATP binding | |
Biological Process | ADP biosynthetic process | |
Biological Process | AMP metabolic process | |
Biological Process | ATP metabolic process | |
Biological Process | phosphorylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenylate kinase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Agaricales > Marasmiineae > Physalacriaceae > Armillaria
Accessions
- Primary accessionA0A2H3DA29
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Predominantly mitochondrial.
Keywords
- Cellular component
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 68-97 | NMPbind | ||||
Sequence: ATGDMLREQVTAKTALGVEAKKIMDAGGLV | ||||||
Region | 165-202 | LID | ||||
Sequence: GRLIHPASGRSYHKEFHPPKKPMTDDITGEPLIQRSDD | ||||||
Domain | 166-201 | Adenylate kinase active site lid | ||||
Sequence: RLIHPASGRSYHKEFHPPKKPMTDDITGEPLIQRSD |
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. AK2 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length255
- Mass (Da)28,096
- Last updated2018-01-31 v1
- ChecksumB3098BCB58138A02
Keywords
- Technical term