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CATH Superfamily 3.30.413.10

Sulfite Reductase Hemoprotein, domain 1

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:

"
Sulfite Reductase Hemoprotein, domain 1
".

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 240: Sulfite reductase, dissimilatory-type alpha subuni...

There are 3 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
Transferred entry: 1.8.99.5. [EC: 1.8.99.3]
    		2 F9UDB2 G2E173
    Deleted entry. [EC: 1.8.99.1]
      		1 I3Y6I5
      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
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