CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.3210 | Hypothetical protein af1432 |
|
1.10.3210.10 | Hypothetical protein af1432 |
Domain Context
CATH Clusters
| Superfamily | Hypothetical protein af1432 |
| Functional Family | Metal dependent phosphohydrolase |
Enzyme Information
| 3.1.3.89 |
5'-deoxynucleotidase.
based on mapping to UniProt P76491
A 2'-deoxyribonucleoside 5'-monophosphate + H(2)O = a 2'-deoxyribonucleoside + phosphate.
-!- The enzyme, characterized from the bacterium Escherichia coli, shows strict specificity toward deoxyribonucleoside 5'-monophosphates and does not dephosphorylate 5'-ribonucleotides or ribonucleoside 3'-monophosphates.
|
| 3.1.3.5 |
5'-nucleotidase.
based on mapping to UniProt P76491
A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate.
-!- Wide specificity for 5'-nucleotides.
|
UniProtKB Entries (1)
| P76491 |
5DNU_ECOLI
Escherichia coli K-12
5'-deoxynucleotidase YfbR
|
PDB Structure
| PDB | 2PAQ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli.
J.Mol.Biol.
|