HAMAP rule MF_00060
General rule information
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Accession | MF_00060 |
Dates | 1-JUN-2001 (Created) 19-NOV-2022 (Last updated, Version 40) |
Name | SurE |
Scope | Bacteria
Archaea |
Templates | P96112 (SURE_THEMA); P0A840 (SURE_ECOLI); Q8ZU79 (SURE1_PYRAE): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
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case <OC:Enterobacterales>
Protein name |
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end case
case not <OC:Enterobacterales>
Protein name |
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end case
Gene name |
|
Comments
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case <OC:Enterobacterales>
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 | RHEA:12484: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
EC 3.1.3.5 |
RHEA:10144: a ribonucleoside 3'-phosphate + H2O = a ribonucleoside + phosphate
EC 3.1.3.6 |
|
RHEA:21528: [phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate
EC 3.6.1.11 |
end case
case not <OC:Enterobacterales>
Function | Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. |
Catalytic activity | RHEA:12484: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
EC 3.1.3.5 |
end case
Cofactor | a divalent metal cation Note: Binds 1 divalent metal cation per subunit. |
Subcellular location | Cytoplasm. |
Similarity | Belongs to the SurE nucleotidase family. |
Keywords
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Gene Ontology
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GO:0008253; Molecular function: 5'-nucleotidase activity.
case <OC:Enterobacterales>
GO:0004309; Molecular function: exopolyphosphatase activity.
GO:0008254; Molecular function: 3'-nucleotidase activity.
GO:0008254; Molecular function: 3'-nucleotidase activity.
end case
Cross-references
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Features
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From: SURE_THEMA (P96112) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 8 | 8 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240 | D | ||||||||
BINDING | 9 | 9 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240 | D | ||||||||
BINDING | 39 | 39 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240 | S | ||||||||
BINDING | 95 | 95 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240 | N |
Additional information
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Size range | 244-283 amino acids |
Related rules | None |
Fusion | None |
Comments | In some organisms, surE was originally annotated as an acid phosphatase (EC 3.1.3.2). Weird C-terminal sequence in TREPA; no obvious frameshift; not shown in alignment and not used in size range. There are divergent second copies of surE in NOSS1 (alr3139) and SYNY3 (sll1459). |