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Information on EC 2.1.1.98 - diphthine synthase and Organism(s) Aeropyrum pernix and UniProt Accession Q9YDI2

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.98 diphthine synthase
IUBMB Comments
This archaeal enzyme produces the trimethylated product diphthine, which is converted into diphthamide by EC 6.3.1.14, diphthine---ammonia ligase. 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 His600 of elongation factor 2.
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Aeropyrum pernix
UNIPROT: Q9YDI2
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The taxonomic range for the selected organisms is: Aeropyrum pernix
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Synonyms
diphthine synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diphthine methyltransferase
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methyltransferase, diphthine
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S-adenosyl-L-methionine:elongation factor 2 methyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] methyltransferase (diphthine-[translation elongation factor 2]-forming)
This archaeal enzyme produces the trimethylated product diphthine, which is converted into diphthamide by EC 6.3.1.14, diphthine---ammonia ligase. 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 His600 of elongation factor 2.
CAS REGISTRY NUMBER
COMMENTARY hide
114514-25-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31500
2 * 31500, calculated from sequence, crystallographic data, only one of the two active sites binds the reaction product S-adenosyl-L-homocysteine, while the other active site contains no ligand
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 31500, calculated from sequence, crystallographic data, only one of the two active sites binds the reaction product S-adenosyl-L-homocysteine, while the other active site contains no ligand
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method at 20°C, structure is resolved at 2.0 A resolution. The homodimeric crystal structures of the archaeal diphthine synthases from Pyrococcus horikoshii DSM 12428 and Aeropyrum pernix DSM 11879 share the same overall fold as the cobalt-precorrin-4 methyltransferase CbiF
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kishishita, S.; Shimizu, K.; Murayama, K.; Terada, T.; Shirouzu, M.; Yokoyama, S.; Kunishima, N.
Structures of two archaeal diphthine synthases: insights into the post-translational modification of elongation factor 2
Acta Crystallogr. Sect. D
64
397-406
2008
Aeropyrum pernix (Q9YDI2), Aeropyrum pernix DSM 11879 (Q9YDI2), Pyrococcus horikoshii (O58456), Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428 (O58456)
Manually annotated by BRENDA team