Q9D8W6 · Q9D8W6_MOUSE
- ProteinGTP:AMP phosphotransferase AK3, mitochondrial
- GeneAk3
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids189 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities.
Catalytic activity
- a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'-diphosphate + ADP
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 17-22 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GSGKGT | ||||||
Binding site | 38 | AMP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 43 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 64-66 | AMP (UniProtKB | ChEBI) | ||||
Sequence: KLI | ||||||
Binding site | 91-94 | AMP (UniProtKB | ChEBI) | ||||
Sequence: GFPR | ||||||
Binding site | 98 | AMP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 128 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 137-138 | GTP (UniProtKB | ChEBI) | ||||
Sequence: VY | ||||||
Binding site | 161 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 172 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Molecular Function | adenylate kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | GTP binding | |
Molecular Function | nucleoside diphosphate kinase activity | |
Molecular Function | nucleoside triphosphate adenylate kinase activity | |
Biological Process | ADP biosynthetic process | |
Biological Process | AMP metabolic process | |
Biological Process | GTP metabolic process | |
Biological Process | ITP metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGTP:AMP phosphotransferase AK3, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9D8W6
Organism-specific databases
Subcellular Location
PTM/Processing
Proteomic databases
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 37-66 | NMPbind | ||||
Sequence: SSGDLLRQNMLQGTEIGVLAKTFIDQGKLI | ||||||
Region | 127-164 | LID | ||||
Sequence: ARWIHPASGRVYNIEFNPPKTVGIDDLTGEPLIQREDD | ||||||
Domain | 128-163 | Adenylate kinase active site lid | ||||
Sequence: RWIHPASGRVYNIEFNPPKTVGIDDLTGEPLIQRED |
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 GTP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent GTP hydrolysis.
Sequence similarities
Belongs to the adenylate kinase family. AK3 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length189
- Mass (Da)21,194
- Last updated2001-06-01 v1
- Checksum822ADB21804F5336