A0A140VK93 · A0A140VK93_HUMAN
- ProteinAdenylate kinase 2, mitochondrial
- GeneAK2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids239 (go to sequence)
- Protein existenceEvidence at transcript level
- 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. Plays a key role in hematopoiesis.
Catalytic activity
- AMP + ATP = 2 ADP
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 25-30 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GAGKGT | ||||||
Binding site | 46 | AMP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 51 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 72-74 | AMP (UniProtKB | ChEBI) | ||||
Sequence: KLV | ||||||
Binding site | 100-103 | AMP (UniProtKB | ChEBI) | ||||
Sequence: GFPR | ||||||
Binding site | 107 | AMP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 142 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 151-152 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SY | ||||||
Binding site | 175 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 186 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 214 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial intermembrane space | |
Cellular Component | sperm mitochondrial sheath | |
Molecular Function | adenylate kinase activity | |
Molecular Function | ATP binding | |
Biological Process | ADP biosynthetic process | |
Biological Process | AMP metabolic process | |
Biological Process | ATP metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenylate kinase 2, mitochondrial
- EC number
- Short namesAK 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A140VK93
Organism-specific databases
Subcellular Location
Disease & Variants
Organism-specific databases
PTM/Processing
Features
Showing features for initiator methionine, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Disulfide bond | 42↔92 | |||||
Sequence: CHLATGDMLRAMVASGSELGKKLKATMDAGKLVSDEMVVELIEKNLETPLC |
Keywords
- PTM
Expression
Gene expression databases
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 45-74 | NMPbind | ||||
Sequence: ATGDMLRAMVASGSELGKKLKATMDAGKLV | ||||||
Region | 141-178 | LID | ||||
Sequence: GRLIHPKSGRSYHEEFNPPKEPMKDDITGEPLIRRSDD | ||||||
Domain | 142-177 | Adenylate kinase active site lid | ||||
Sequence: RLIHPKSGRSYHEEFNPPKEPMKDDITGEPLIRRSD | ||||||
Region | 150-169 | Disordered | ||||
Sequence: RSYHEEFNPPKEPMKDDITG |
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
- Length239
- Mass (Da)26,478
- Last updated2016-06-08 v1
- Checksum86FA94F9EE33629F
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HM005633 EMBL· GenBank· DDBJ | AEE61230.1 EMBL· GenBank· DDBJ | mRNA |