| Accession |
MF_00060 |
| Dates |
1-JUN-2001 (Created) 9-DEC-2011 (Last updated, Version 31) |
case <OC:Enterobacteriaceae>
| Protein name |
| RecName: |
Full=5'/3'-nucleotidase SurE; EC=3.1.3.5; EC=3.1.3.6; |
| AltName: |
Full=Exopolyphosphatase; EC=3.6.1.11; |
| AltName: |
Full=Nucleoside monophosphate phosphohydrolase; |
|
end case
case not <OC:Enterobacteriaceae>
| Protein name |
| RecName: |
Full=5'-nucleotidase surE; EC=3.1.3.5; |
| AltName: |
Full=Nucleoside 5'-monophosphate phosphohydrolase; |
|
end case
case <OC:Enterobacteriaceae>
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 (By similarity).
CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate.
CATALYTIC ACTIVITY: A 3'-ribonucleotide + H(2)O = a ribonucleoside + phosphate.
CATALYTIC ACTIVITY: (Polyphosphate)(n) + H(2)O = (polyphosphate)(n-1) + phosphate.
end case
case not <OC:Enterobacteriaceae>
FUNCTION: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates (By similarity).
CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate.
end case
COFACTOR: Binds 1 divalent metal cation per subunit (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (Potential).
SIMILARITY: Belongs to the surE nucleotidase family.
GO:0008253; Molecular function: 5'-nucleotidase activity.
case <OC:Enterobacteriaceae>
GO:0004309; Molecular function: exopolyphosphatase activity.
GO:0008254; Molecular function: 3'-nucleotidase activity.
end case
| From: SURE_THEMA (P96112) |
| Key |
|
From |
|
To |
|
Description |
|
Condition |
|
FTGroup |
| METAL |
|
8 |
|
8 |
|
Divalent metal cation (By similarity) |
|
D |
|
|
| METAL |
|
9 |
|
9 |
|
Divalent metal cation (By similarity) |
|
D |
|
|
| METAL |
|
39 |
|
39 |
|
Divalent metal cation (By similarity) |
|
S |
|
|
| METAL |
|
95 |
|
95 |
|
Divalent metal cation (By similarity) |
|
N |
|
|
| Size range: |
244-283 amino acids |
| Related UniRules: |
None |
| Template: |
P96112 (SURE_THEMA); P0A840 (SURE_ECOLI); Q8ZU79 (SURE1_PYRAE): [Recover all] |
| Scope: |
Bacteria
Archaea |
| Fusion: |
Nter: None; Cter: None |
| Duplicate: |
in BURS3, CHLCV, PYRAE, THET2 |
| Plasmid encoded: |
in THET2, THET8 |
| 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). |
View rule in raw text format (no links)