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CATH Superfamily 3.40.50.620

HUPs

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:

"
HUPs
".

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.
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FunFam 89152: Cytoplasmic tRNA 2-thiolation protein 1

There are 4 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
Cysteine desulfurase. [EC: 2.8.1.7]
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.
  • The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors.
  • The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin).
  • In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation.
 12 A0A074TKS9 A0A086JIP2 A0A086JTR4 A0A086KRA6 A0A086LSA6 A0A086PSJ4 A0A086QNX8 A0A125YK15 A0A139XLS1 A0A151H930
(2 more...)
TRNA sulfurtransferase. [EC: 2.8.1.4]
L-cysteine + 'activated' tRNA = L-serine + tRNA containing a thionucleotide.
  • A group of enzymes transferring sulfur to various nucleotides in a tRNA chain, producing residues such as 4-thiouridylate.
  • With some enzymes mercaptopyruvate can act as sulfur donor.
 5 H2CFU5 I4B8F4 K8GM74 K9F1B1 K9WKS1
TRNA(Ile)-lysidine synthetase. [EC: 6.3.4.19]
(tRNA(Ile2))-cytidine(34) + L-lysine + ATP = (tRNA(Ile2))-lysidine(34) + AMP + diphosphate + H(2)O.
  • The bacterial enzyme modifies the wobble base of the CAU anticodon of tRNA(Ile) at the oxo group in position 2 of cytidine(34).
  • This modification determines both codon and amino acid specificities of tRNA(Ile).
 2 A0A0C2Z9Q1 R5ELL7
Hypoxanthine phosphoribosyltransferase. [EC: 2.4.2.8]
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate.
  • Guanine and 6-mercaptopurine can replace hypoxanthine.
 2 A0A087RP58 A0A087S433
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