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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 79831: Type II peroxiredoxin F

There are 9 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
Peroxiredoxin. [EC: 1.11.1.15]
2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
  • Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins.
  • They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins.
  • The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine.
  • All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid).
  • The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes.
  • For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), completing the catalytic cycle.
  • In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond.
  • To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor.
  • The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule.
 1572 A0A011PPK2 A0A011PPK2 A0A011R415 A0A011R415 A0A021X1T4 A0A021X1T4 A0A024V8F8 A0A024V8F8 A0A024VSZ6 A0A024VSZ6
(1562 more...)
Glutathione amide-dependent peroxidase. [EC: 1.11.1.17]
2 glutathione amide + H(2)O(2) = glutathione amide disulfide + 2 H(2)O.
  • This enzyme, which has been characterized from the proteobacterium Marichromatium gracile, is a chimeric protein, containing a peroxiredoxin-like N-terminus and a glutaredoxin-like C terminus.
  • The enzyme has peroxidase activity toward hydrogen peroxide and several small alkyl hydroperoxides, and is thought to represent an early adaptation for fighting oxidative stress.
  • The glutathione amide disulfide produced by this enzyme can be restored to glutathione amide by EC 1.8.1.16.
 32 A0A0H0XWZ1 A0A0H0XWZ1 A0A0N0GNI5 A0A0N0GNI5 A0A0N8TTZ1 A0A0N8TTZ1 A0A0Q0GZZ4 A0A0Q0GZZ4 A0A165YE51 A0A165YE51
(22 more...)
Cytochrome-c peroxidase. [EC: 1.11.1.5]
2 ferrocytochrome c + H(2)O(2) = 2 ferricytochrome c + 2 H(2)O.
    		 30 A0A0A0HKV3 A0A0A0HKV3 A0A0H4KYZ3 A0A0H4KYZ3 A0A0J5Q903 A0A0J5Q903 A0A0P7XJ83 A0A0P7XJ83 A0A0P7Y2N9 A0A0P7Y2N9
    (20 more...)
    Arsenate reductase (glutaredoxin). [EC: 1.20.4.1]
    Arsenate + glutaredoxin = arsenite + glutaredoxin disulfide + H(2)O.
    • The enzyme is part of a system for detoxifying arsenate.
    • Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 3.6.3.16; in other organisms, arsenite can be methylated by EC 2.1.1.137 in a pathway that produces non-toxic organoarsenical compounds (cf. EC 1.20.4.4).
    • Formerly EC 1.97.1.5.
    		 12 A0A0J6LJK3 A0A0J6LJK3 A0A157M617 A0A157M617 A0A157R8G6 A0A157R8G6 A0A157SWK8 A0A157SWK8 A9INX5 A9INX5
    (2 more...)
    Peroxidase. [EC: 1.11.1.7]
    2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O.
      		 10 A0A085U3J5 A0A085U3J5 A0A1M4L9F3 A0A1M4L9F3 C8CG65 C8CG65 D1CW43 D1CW43 E2PPI7 E2PPI7
      Amino-acid N-acetyltransferase. [EC: 2.3.1.1]
      Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.
      • Also acts with L-aspartate and, more slowly, with some other amino acids.
      		 2 A8T9N1 A8T9N1
      Peptidylprolyl isomerase. [EC: 5.2.1.8]
      Peptidylproline (omega=180) = peptidylproline (omega=0).
      • The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A.
      • Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli.
      • The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.
      		 2 A0A176W0D8 A0A176W0D8
      Nicotinate-nucleotide adenylyltransferase. [EC: 2.7.7.18]
      ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD(+).
        		 2 U2XMJ7 U2XMJ7
        Proteasome endopeptidase complex. [EC: 3.4.25.1]
        Cleavage of peptide bonds with very broad specificity.
        • A 20-S protein composed of 28 subunits arranged in four rings of seven.
        • The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity.
        • In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities.
        • The molecule is barrel-shaped, and the active sites are on the inner surfaces.
        • Terminal apertures restrict access of substrates to the active sites.
        • Inhibited by mercurial reagents and some inhibitors of serine endopeptidases.
        • Belongs to peptidase family T1.
        • Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46.
        		 2 A0A075B4S9 A0A075B4S9