Q5JCX3 · AMPPA_THEKO
- ProteinAMP phosphorylase
- GenedeoA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids503 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP, dCMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.
Catalytic activity
- AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate
Activity regulation
AMP phosphorolysis is allosterically regulated by the substrate AMP.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
6.2 mM | CMP | 85 | in the presence of AMP | |||
4.4 mM | UMP | 85 | in the presence of AMP | |||
18.5 mM | GMP | 85 | in the presence of AMP | |||
2.8 mM | phosphate | 85 | in the presence of AMP |
kcat is 39.1 sec-1, 15.0 sec-1, 10.5 sec-1 and 2.7 sec-1, with CMP, AMP, UMP, and GMP as substrate, respectively (at 85 degrees Celsius). KM for AMP was not determined because the reaction does not follow Michaelis-Menten kinetics.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 168 | AMP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 194-199 | AMP (UniProtKB | ChEBI) | ||||
Sequence: SRAITS | ||||||
Binding site | 203 | AMP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Active site | 256 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 264 | AMP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 288 | AMP (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | 1,4-alpha-oligoglucan phosphorylase activity | |
Molecular Function | AMP binding | |
Molecular Function | pentosyltransferase activity | |
Molecular Function | phosphate ion binding | |
Biological Process | AMP catabolic process | |
Biological Process | pyrimidine deoxyribonucleoside metabolic process | |
Biological Process | pyrimidine nucleobase metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAMP phosphorylase
- EC number
- Short namesAMPpase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Thermococci > Thermococcales > Thermococcaceae > Thermococcus
Accessions
- Primary accessionQ5JCX3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 256 | Almost complete loss of activity. | ||||
Sequence: D → N or A | ||||||
Mutagenesis | 288 | Almost complete loss of activity. | ||||
Sequence: K → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000059093 | 1-503 | AMP phosphorylase | |||
Sequence: MKAKIRILDMFSGRYTVLINEEDAKEAKLHPDDLVKIEAGKKAVYGSVALSNLVGKGEVGISRDVLDLHNFSEGETVSVIPAGTPESVRYIKKKMHGEKLRKVEIEAIVRDIVDRKLRDIEISSFVTALEINGLDMDEIAALTIAMAETGDMLDIDRKPIMDVHSIGGVPGNKTNILVVPIVAAAGLTIPKTSSRAITSAAGTADVVEVFADVSFSLDEIKRIVEKVGACLVWGGALNLAPADDITIKAERALSIDPTGLMLASIMSKKYAMGSQYVLIDIPTGKGVKVETVEEARSLARDFIELGKRLGQYVEVAITYGGQPIGHTVGPALEAREALSALMTGKGPGSLIEKATGLAGILLEMGGVAPAGTGKKMAKEILESGKAWEKMKEIIEAQGGDPNIKPEEIPIGDKTYTFTAATSGYVTAIDNRAITAIARAAGAPEDKGAGIELYVKVGEKVKEGDPLFTIHAEHEARLDQAIVLARRTEPIRIEGMVLQRIGNI |
Expression
Induction
Constitutively expressed (at protein level). Does not respond to the addition of nucleosides.
Interaction
Subunit
Forms an exceptionally large macromolecular structure (>40-mers) in solution.
Protein-protein interaction databases
Structure
Family & Domains
Domain
The N-terminal domain (residues 1-84), characteristic of archaeal AMPpases, is essential for enzymatic activity, participating in multimerization as well as domain closure of the active site upon substrate binding. Harbors two dimer interfaces within a single molecule: one by the central domain and the other by the C-terminal domain; these two interactions can continuously occur in a repetitive manner, leading to multimerization.
Sequence similarities
Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length503
- Mass (Da)53,651
- Last updated2005-02-15 v1
- Checksum63AB57AE279ACCBA
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP006878 EMBL· GenBank· DDBJ | BAD84541.1 EMBL· GenBank· DDBJ | Genomic DNA |