CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.70 | Aldolase class I |
Domain Context
CATH Clusters
| Superfamily | Aldolase class I |
| Functional Family | 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase |
Enzyme Information
| 5.3.1.16 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase.
based on mapping to UniProt P16250
1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D- ribosylamino)methylideneamino)imidazole-4-carboxamide = 5-((5-phospho-1- deoxy-D-ribulos-1-ylamino)methylideneamino)-1-(5-phospho-beta-D- ribosyl)imidazole-4-carboxamide.
-!- Involved in histidine biosynthesis.
|
| 5.3.1.24 |
Phosphoribosylanthranilate isomerase.
based on mapping to UniProt P16250
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1- deoxy-D-ribulose 5-phosphate.
-!- In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 2.4.2.18, EC 4.1.1.48, EC 4.1.3.27 and EC 4.2.1.20).
|
UniProtKB Entries (1)
| P16250 |
HIS4_STRCO
Streptomyces coelicolor A3(2)
Phosphoribosyl isomerase A
|
PDB Structure
| PDB | 5DN1 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Co-occurrence of analogous enzymes determines evolution of a novel ( beta alpha )8-isomerase sub-family after non-conserved mutations in flexible loop.
Biochem. J.
|
