CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.60 | Sandwich |
|
2.60.120 | Jelly Rolls |
|
2.60.120.10 | Jelly Rolls |
Domain Context
CATH Clusters
| Superfamily | Jelly Rolls |
| Functional Family |
Enzyme Information
| 2.4.2.3 |
Uridine phosphorylase.
based on mapping to UniProt Q6FF51
Uridine + phosphate = uracil + alpha-D-ribose 1-phosphate.
-!- The enzyme participates the the pathways of pyrimidine ribonucleosides degradation and salvage. -!- The mammalian enzyme also accepts 2'-deoxyuridine. -!- Formerly EC 2.4.2.23.
|
| 2.4.2.15 |
Guanosine phosphorylase.
based on mapping to UniProt Q6FF51
Guanosine + phosphate = guanine + alpha-D-ribose 1-phosphate.
-!- Also acts on deoxyguanosine.
|
| 2.4.2.2 |
Pyrimidine-nucleoside phosphorylase.
based on mapping to UniProt Q6FF51
(1) Uridine + phosphate = uracil + alpha-D-ribose 1-phosphate. (2) Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate. (3) 2'-deoxyuridine + phosphate = uracil + 2-deoxy-alpha-D-ribose 1-phosphate.
-!- Unlike EC 2.4.2.3 and EC 2.4.2.4, this enzyme can accept both the ribonucleoside uridine and the 2'-deoxyribonucleosides 2'-deoxyuridine and thymidine. -!- The reaction is reversible, and the enzyme does not distinguish between alpha-D-ribose 1-phosphate and 2-deoxy-alpha-D-ribose 1-phosphate in the synthetic direction. -!- Formerly EC 2.4.2.23.
|
| 2.4.2.4 |
Thymidine phosphorylase.
based on mapping to UniProt Q6FF51
Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate.
-!- In some tissues also catalyzes deoxyribosyltransferase reactions of the type catalyzed by EC 2.4.2.6. -!- Formerly EC 2.4.2.23.
|
UniProtKB Entries (1)
| Q6FF51 |
PPNP_ACIAD
Acinetobacter baylyi ADP1
Pyrimidine/purine nucleoside phosphorylase
|
PDB Structure
| PDB | 3HQX |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of protein of unknown function (DUF1255,PF06865) from Acinetobacter sp. ADP1
To be Published
|
