1 keywords

CATH Domain 1vhvA02

CATH Classification

Level CATH Code Description
Class 3 Alpha Beta
Architecture 3.30 2-Layer Sandwich
Topology 3.30.950 Methyltransferase, Cobalt-precorrin-4 Transmethylase; Domain 2
Homologous Superfamily 3.30.950.10 Methyltransferase, Cobalt-precorrin-4 Transmethylase; Domain 2

Domain Context

CATH Clusters

Superfamily Methyltransferase, Cobalt-precorrin-4 Transmethylase; Domain 2
Functional Family

Enzyme Information

2.1.1.98
Diphthine synthase.
based on mapping to UniProt O29866
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)

O29866
DPHB_ARCFU
Archaeoglobus fulgidus DSM 4304
Diphthine synthase

PDB Structure

PDB 1VHV
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structural analysis of a set of proteins resulting from a bacterial genomics project
Badger, J., Sauder, J.M., Adams, J.M., Antonysamy, S., Bain, K., Bergseid, M.G., Buchanan, S.G., Buchanan, M.D., Batiyenko, Y., Christopher, J.A., Emtage, S., Eroshkina, A., Feil, I., Furlong, E.B., Gajiwala, K.S., Gao, X., He, D., Hendle, J., Huber, A., Hoda, K., Kearins, P., Kissinger, C., Laubert, B., Lewis, H.A., Lin, J., Loomis, K., Lorimer, D., Louie, G., Maletic, M., Marsh, C.D., Miller, I., Molinari, J., Muller-Dieckmann, H.J., Newman, J.M., Noland, B.W., Pagarigan, B., Park, F., Peat, T.S., Post, K.W., Radojicic, S., Ramos, A., Romero, R., Rutter, M.E., Sanderson, W.E., Schwinn, K.D., Tresser, J., Winhoven, J., Wright, T.A., Wu, L., Xu, J., Harris, T.J.
Proteins