CATH Domain 1vkyA02

CATH Classification

Level	CATH Code	Description
	2	Mainly Beta
	2.40	Beta Barrel
	2.40.10	Thrombin, subunit H
	2.40.10.240	QueA-like

Domain Context

CATH Clusters

Superfamily	QueA-like
Functional Family	S-adenosylmethionine:tRNA ribosyltransferase-isomerase

Enzyme Information

2.4.99.17

S-adenosylmethionine:tRNA ribosyltransferase-isomerase.

based on mapping to UniProt Q9WZ44

S-adenosyl-L-methionine + 7-aminomethyl-7-carbaguanosine(34) in tRNA = L-methionine + adenine + epoxyqueuosine(34) in tRNA.

-!- The reaction is a combined transfer and isomerization of the ribose moiety of S-adenosyl-L-methionine to the modified guanosine base in the wobble position in tRNAs specific for Tyr, His, Asp or Asn. -!- It is part of the queuosine biosynthesis pathway.

UniProtKB Entries (1)

Q9WZ44

QUEA_THEMA

Thermotoga maritima MSB8

S-adenosylmethionine:tRNA ribosyltransferase-isomerase

PDB Structure

PDB	1VKY
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Crystal structure of S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) from Thermotoga maritima at 2.0 A resolution reveals a new fold. Mathews, I., Schwarzenbacher, R., McMullan, D., Abdubek, P., Ambing, E., Axelrod, H., Biorac, T., Canaves, J.M., Chiu, H.J., Deacon, A.M., DiDonato, M., Elsliger, M.A., Godzik, A., Grittini, C., Grzechnik, S.K., Hale, J., Hampton, E., Han, G.W., Haugen, J., Hornsby, M., Jaroszewski, L., Klock, H.E., Koesema, E., Kreusch, A., Kuhn, P., Lesley, S.A., Levin, I., Miller, M.D., Moy, K., Nigoghossian, E., Ouyang, J., Paulsen, J., Quijano, K., Reyes, R., Spraggon, G., Stevens, R.C., van den Bedem, H., Velasquez, J., Vincent, J., White, A., Wolf, G., Xu, Q., Hodgson, K.O., Wooley, J., Wilson, I.A. Proteins