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UniProt functional annotation for O58456 | ||
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| UniProt code: O58456. |
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| Organism: | |
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3). |
| Taxonomy: | |
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; Pyrococcus. |
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| 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. {ECO:0000255|HAMAP-Rule:MF_01084, ECO:0000269|PubMed:20873788}. |
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| Catalytic activity: | |
Reaction=2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine- [translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L- homocysteine; Xref=Rhea:RHEA:36415, Rhea:RHEA-COMP:9749, Rhea:RHEA- COMP:10172, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73995, ChEBI:CHEBI:82696; EC=2.1.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_01084, ECO:0000269|PubMed:20873788}; |
| Pathway: | |
Protein modification; peptidyl-diphthamide biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01084, ECO:0000269|PubMed:20873788}. |
| Subunit: | |
Homodimer. {ECO:0000255|HAMAP-Rule:MF_01084, ECO:0000269|PubMed:18391406, ECO:0000269|Ref.4}. |
| Miscellaneous: | |
The diphthine intermediate is not stable in vitro and readily eliminates the trimethylamino group. It is not known whether the elimination reaction also occurs physiologically. |
| Similarity: | |
Belongs to the diphthine synthase family. {ECO:0000255|HAMAP-Rule:MF_01084, ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.