A0A014NMB1 · A0A014NMB1_9GAMM
- Protein5'/3'-nucleotidase SurE
- GenesurE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids253 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs.
Catalytic activity
- [phosphate](n) + H2O = [phosphate](n-1) + phosphate + H+
[phosphate](n) RHEA-COMP:9859 + CHEBI:15377 = [phosphate](n-1) RHEA-COMP:14279 + CHEBI:43474 + CHEBI:15378
Cofactor
Note: Binds 1 divalent metal cation per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 8 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 9 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 39 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 92 | a divalent metal cation (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 3'-nucleotidase activity | |
Molecular Function | exopolyphosphatase activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleotide binding | |
Molecular Function | XMP 5'-nucleosidase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name5'/3'-nucleotidase SurE
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Erwiniaceae > Erwinia
Accessions
- Primary accessionA0A014NMB1
Proteomes
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length253
- Mass (Da)27,112
- Last updated2014-06-11 v1
- Checksum9D0AB41920B35CF1
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JFHN01000053 EMBL· GenBank· DDBJ | EXU74945.1 EMBL· GenBank· DDBJ | Genomic DNA |