View in Gene3D

CATH Superfamily 2.40.30.10

Translation factors

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Translation factors
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
« Back to all FunFams

FunFam 38326: Mitochondrial tRNA-specific 2-thiouridylase 1

There are 5 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
TRNA-uridine 2-sulfurtransferase. [EC: 2.8.1.13]
A [protein]-S-sulfanyl-L-cysteine + uridine(34) in tRNA + ATP + reduced acceptor = a [protein]-L-cysteine + 2-thiouridine(34) in tRNA + AMP + diphosphate + acceptor.
  • The enzyme, found in bacteria, catalyzes formation of the 2-thiouridine modification in the wobble position of tRNA(Gln), tRNA(Lys) and tRNA(Glu).
 1282 A0A011Q650 A0A014NQI8 A0A015KRQ0 A0A023CKR1 A0A031JYT6 A0A060M0B4 A0A060QE00 A0A060R9X9 A0A062X7V0 A0A063YCG8
(1272 more...)
TRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase. [EC: 2.1.1.61]
S-adenosyl-L-methionine + tRNA containing 5-aminomethyl-2-thiouridine = S-adenosyl-L-homocysteine + tRNA containing 5-methylaminomethyl-2- thiouridylate.
  • Specific for the terminal methyl group of 5-methylaminomethyl-2- thiouridylate.
 3 A0A1K1P1L3 B8IYA5 H5VEA8
Riboflavin kinase. [EC: 2.7.1.26]
ATP + riboflavin = ADP + FMN.
  • The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B(6), vitamin B12 and folates.
  • While monofunctional riboflavin kinase is found in eukaryotes, some bacteria have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.7.2.
  • In Bacillus subtilis, ATP can be replaced by other phosphate donors but with decreasing enzyme activity in the order ATP > dATP > CTP > UTP.
 1 Q7NBZ0
FAD synthetase. [EC: 2.7.7.2]
ATP + FMN = diphosphate + FAD.
  • Highly specific for ATP as phosphate donor.
  • The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates.
  • While monofunctional FAD synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.1.26.
 1 Q7NBZ0
TRNA-5-taurinomethyluridine 2-sulfurtransferase. [EC: 2.8.1.14]
A [protein]-S-sulfanyl-L-cysteine + 5-taurinomethyluridine(34) in tRNA + ATP + reduced acceptor = a [protein]-L-cysteine + 5-taurinomethyl-2- thiouridine(34) in tRNA + AMP + diphosphate + acceptor.
  • The enzyme, found in mitochondria, catalyzes formation of 5-taurinomethyl-2-thiouridine in the wobble position of mitochondrial tRNA(Gln), tRNA(Lys) and tRNA(Glu).
 1 O13947
CATH-Gene3D is a Global Biodata Core Resource Learn more...