A0A1Z2TP61 · A0A1Z2TP61_9EURY
- ProteinDiphthine synthase
- GenedphB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids264 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.
Catalytic activity
- 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 S-adenosyl-L-homocysteine + 3 H+
Pathway
Protein modification; peptidyl-diphthamide biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 10 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 87 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 90 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 115-116 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: SI | ||||||
Binding site | 166 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 209 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 234 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | diphthine synthase activity | |
Biological Process | methylation | |
Biological Process | protein histidyl modification to diphthamide |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDiphthine synthase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Thermococci > Thermococcales > Thermococcaceae > Thermococcus
Accessions
- Primary accessionA0A1Z2TP61
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-213 | Tetrapyrrole methylase | ||||
Sequence: IYFIGLGLYDEKDITLKGLETARKCDLVFAEFYTSLLAGTTLDKVEELIGKPIRRLSREEVELHFERIVLSEAKEKDVAFLTAGDPMVATTHSDLRIRAKELGIESYVIHAPSIYSAIAVTGLQIYKFGKSATVAYPEKNWFPTSHYDVIKENMERNLHTMLFLDIKAEQNRYMTANEAMEILLQVEDMKRENVFTPDTLVVVLARAGSLN |
Sequence similarities
Belongs to the diphthine synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length264
- Mass (Da)29,828
- Last updated2017-09-27 v1
- ChecksumA3981DC24E15B3C1
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP021848 EMBL· GenBank· DDBJ | ASA78235.1 EMBL· GenBank· DDBJ | Genomic DNA |