A0A8H4S0D7 · A0A8H4S0D7_9EURO
- ProteinGTP:AMP phosphotransferase, mitochondrial
- GeneADK2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids255 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 | 21-26 | GTP (UniProtKB | ChEBI) | |||
Binding site | 43 | AMP (UniProtKB | ChEBI) | |||
Binding site | 48 | AMP (UniProtKB | ChEBI) | |||
Binding site | 69-71 | AMP (UniProtKB | ChEBI) | |||
Binding site | 129-132 | AMP (UniProtKB | ChEBI) | |||
Binding site | 136 | AMP (UniProtKB | ChEBI) | |||
Binding site | 166 | GTP (UniProtKB | ChEBI) | |||
Binding site | 175-176 | GTP (UniProtKB | ChEBI) | |||
Binding site | 199 | AMP (UniProtKB | ChEBI) | |||
Binding site | 210 | AMP (UniProtKB | ChEBI) | |||
Binding site | 239 | GTP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Molecular Function | adenylate kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | GTP binding | |
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 | |
Biological Process | phosphorylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGTP:AMP phosphotransferase, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium
Accessions
- Primary accessionA0A8H4S0D7
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 42-71 | NMPbind | |||
Region | 91-117 | Disordered | |||
Compositional bias | 92-117 | Polar residues | |||
Region | 165-202 | LID | |||
Domain | 166-201 | Adenylate kinase active site lid | |||
Region | 178-198 | Disordered | |||
Compositional bias | 183-198 | Basic and acidic residues | |||
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
- Length255
- Mass (Da)28,014
- Last updated2022-01-19 v1
- MD5 Checksum3DD60A0BAE418CEC6CC75CB08A852207
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 92-117 | Polar residues | |||
Compositional bias | 183-198 | Basic and acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAASRZ010000051 EMBL· GenBank· DDBJ | KAF4760271.1 EMBL· GenBank· DDBJ | Genomic DNA |