Q2G297 · AP4AH_STAA8
- ProteinBis(5'-nucleosyl)-tetraphosphatase, symmetrical
- GeneyqeK
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids194 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) to yield ADP (PubMed:32152217).
Can also hydrolyze Ap3A, Ap5A, Ap4G, Ap4U and Gp4G, always releasing ADP or GDP as one of the products, but it exhibits a marked preference for Ap4A, which is mainly exerted at the substrate affinity level (PubMed:32152217).
Can also hydrolyze Ap3A, Ap5A, Ap4G, Ap4U and Gp4G, always releasing ADP or GDP as one of the products, but it exhibits a marked preference for Ap4A, which is mainly exerted at the substrate affinity level (PubMed:32152217).
Catalytic activity
- H2O + P1,P4-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H+
Activity regulation
Inhibited by EDTA.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
3.2 μM | Ap4A | |||||
21.5 μM | Ap5A | |||||
19.7 μM | Ap4G | |||||
17.6 μM | Ap4U | |||||
68 μM | Gp4G |
kcat is 107 sec-1 with Ap4A as substrate. kcat is 32 sec-1 with Ap5A as substrate. kcat is 210 sec-1 with Ap4G as substrate. kcat is 324 sec-1 with Ap4U as substrate. kcat is 1002 sec-1 with Gp4G as substrate.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 21 | ADP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 21 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 50 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 51 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 51-54 | ADP (UniProtKB | ChEBI) | ||||
Sequence: DFCK | ||||||
Binding site | 83 | ADP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 109-110 | ADP (UniProtKB | ChEBI) | ||||
Sequence: HT | ||||||
Binding site | 127 | ADP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 127 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 133 | ADP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 172-177 | ADP (UniProtKB | ChEBI) | ||||
Sequence: TVYNKT |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | hydrolase activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleotide binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBis(5'-nucleosyl)-tetraphosphatase, symmetrical
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus
Accessions
- Primary accessionQ2G297
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000454778 | 1-194 | Bis(5'-nucleosyl)-tetraphosphatase, symmetrical | |||
Sequence: MNIEKAKRLAKEKLPEKRYNHSLRVAETAIKLAEIYDGDTSKVELAGVLHDFCKYDDLGKMYQIVRQYELGNDLLSYGSEILHGPVCAAIMEHEYGINDEEVLMAIKYHTTGRQQMTKTEKLIFIADYIEPGRTIPGVDDIRDMAYNQGSLDKTIYEISKRTVLFLIQKDITVYNKTIDCLNYYNYSDERIKDD |
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 18-132 | HD | ||||
Sequence: RYNHSLRVAETAIKLAEIYDGDTSKVELAGVLHDFCKYDDLGKMYQIVRQYELGNDLLSYGSEILHGPVCAAIMEHEYGINDEEVLMAIKYHTTGRQQMTKTEKLIFIADYIEPG |
Sequence similarities
Belongs to the Ap4A hydrolase YqeK family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length194
- Mass (Da)22,464
- Last updated2006-03-21 v1
- Checksum15F2A27F5B5D55FF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000253 EMBL· GenBank· DDBJ | ABD30770.1 EMBL· GenBank· DDBJ | Genomic DNA |