CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.1010 | Cobalt-precorrin-4 Transmethylase; domain 1 |
|
3.40.1010.10 | Cobalt-precorrin-4 Transmethylase; Domain 1 |
Domain Context
CATH Clusters
| Superfamily | Cobalt-precorrin-4 Transmethylase; Domain 1 |
| Functional Family | Putative diphthine synthase |
Enzyme Information
| 2.1.1.98 |
Diphthine synthase.
based on mapping to UniProt O58456
3 S-adenosyl-L-methionine + 2-((3S)-3-carboxy-3-aminopropyl)-L-histidine- [translation elongation factor 2] = 3 S-adenosyl-L-homocysteine + diphthine-[translation elongation factor 2].
-!- This archaeal enzyme produces the trimethylated product diphthine, which is converted into diphthamide by EC 6.3.1.14. -!- Different from the eukaryotic enzyme, which produces diphthine methyl ester (cf. EC 2.1.1.314). -!- In the archaeon Pyrococcus horikoshii the enzyme acts on His(600) of elongation factor 2.
|
UniProtKB Entries (1)
| O58456 |
DPHB_PYRHO
Pyrococcus horikoshii OT3
Diphthine synthase
|
PDB Structure
| PDB | 1WNG |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structures of two archaeal diphthine synthases: insights into the post-translational modification of elongation factor 2.
Acta Crystallogr.,Sect.D
|
