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CATH Superfamily 3.30.70.20

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: waiting to be named.

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 40102: 4Fe-4S ferredoxin, iron-sulfur binding protein

There are 6 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
Pyruvate synthase. [EC: 1.2.7.1]
Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+).
  • The enzyme also decarboxylates 2-oxobutanoate with lower efficiency, but shows no activity with 2-oxoglutarate.
  • This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity.
  • For examples of other members of this family, see EC 1.2.7.3 and EC 1.2.7.7.
 6 A0A0D8W3Z6 A0A0E2LML2 A0A0G3JCT8 A0A0H2YXJ3 B7MID8 Q1RDM5
Transferred entry: 1.8.99.5. [EC: 1.8.99.3]
    		6 A0A1E2ZCP5 A7C7X0 E3HZD3 G2E173 I1X533 S6BZN5
    Nitrate reductase. [EC: 1.7.99.4]
    Nitrite + acceptor = nitrate + reduced acceptor.
    • The Pseudomonas enzyme is a cytochrome, but the enzyme from Micrococcus halodenitrificans is an iron protein containing molybdenum.
    • Reduced benzyl viologen and other dyes bring about the reduction of nitrate.
    		 5 A0A061YNV4 A0A125XJM9 A0A192CJZ5 A0A1L9A2P7 W9ADQ5
    Deleted entry. [EC: 1.8.99.1]
      		2 I3BY25 I3Y6I5
      [Formate-C-acetyltransferase]-activating enzyme. [EC: 1.97.1.4]
      S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical.
      • A single glycine residue in EC 2.3.1.54 is oxidized to the corresponding radical by transfer of H from its CH(2) to AdoMet with concomitant cleavage of the latter.
      • The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5'-yl radical, which then abstracts a hydrogen radical from the glycine residue.
      		 1 A0A1H5T9V3
      Dissimilatory sulfite reductase. [EC: 1.8.99.5]
      (1) Hydrogen sulfide + a [DsrC protein]-disulfide + 2 acceptor + 3 H(2)O = sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H(+). (2) A [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H(2)O = sulfite + a [DsrC protein]-disulfide + 3 reduced acceptor + 2 H(+).
      • The enzyme is essential in prokaryotic sulfur-based energy metabolism, including sulfate/sulfite reducing organisms, sulfur- oxidizing bacteria, and organosulfonate reducers.
      • In sulfur reducers it catalyzes the reduction of sulfite to sulfide, while in sulfur oxidizers it catalyzes the opposite reaction.
      • The reaction involves the small protein DsrC, which is present in all the organisms that contain dissimilatory sulfite reductase.
      • During the process an intramolecular disulfide bond is formed between two L-cysteine residues of DsrC.
      • This disulfide can be reduced by a number of proteins including DsrK and TcmB.
      • This enzyme is different from EC 1.8.1.2 and EC 1.8.7.1, which are involved in sulfate assimilation.
      		 1 O33998