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CATH Superfamily 3.40.30.10

Glutaredoxin

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:

"
Glutaredoxin
".

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 79830: Thioredoxin domain-containing protein 2

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
Protein disulfide-isomerase. [EC: 5.3.4.1]
Catalyzes the rearrangement of -S-S- bonds in proteins.
  • Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange.
 8 B0ED12 B0ED12 B0ERJ7 B0ERJ7 B7P2A3 B7P2A3 L0AV83 L0AV83
Malate synthase. [EC: 2.3.3.9]
Acetyl-CoA + H(2)O + glyoxylate = (S)-malate + CoA.
  • The enzyme catalyzes the irreversible condensation of acetyl-CoA with glyoxylate to form (S)-malate.
  • Among other functions, the enzyme participates in the glyoxylate cycle, a modified version of the TCA cycle that bypasses steps that lead to a loss of CO(2).
  • Formerly EC 4.1.3.2.
 4 A0A081CDG9 A0A081CDG9 W3VEN7 W3VEN7
Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase. [EC: 3.5.1.52]
Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.
  • Does not act on (GlcNAc)-Asn, because it requires the presence of more than two amino-acid residues in the substrate (cf. EC 3.5.1.26).
  • Formerly EC 3.2.2.18.
 4 Q5WNE3 Q5WNE3 Q9TW67 Q9TW67
Adenylyl-sulfate reductase (thioredoxin). [EC: 1.8.4.10]
AMP + sulfite + thioredoxin disulfide = 5'-adenylyl sulfate + thioredoxin.
  • Uses adenylyl sulfate, not phosphoadenylyl sulfate, distinguishing this enzyme from EC 1.8.4.8.
  • Uses thioredoxin as electron donor, not glutathione or other donors, distinguishing it from EC 1.8.4.9 and EC 1.8.99.2.
 2 K9P1V0 K9P1V0