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CATH Superfamily 3.40.228.10

Dimethylsulfoxide Reductase, domain 2

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Dimethylsulfoxide Reductase, domain 2
".

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 9: Formate dehydrogenase, alpha subunit, selenocystei...

There are 2 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
Formate dehydrogenase (cytochrome c-553). [EC: 1.17.2.3]
Formate + 2 ferricytochrome c-553 = CO(2) + 2 ferrocytochrome c-553 + H(+).
  • The enzyme has been characterized from the bacterium Desulfovibrio vulgaris.
  • In vitro, yeast cytochrome c, ferricyanide and phenazine methosulfate can act as acceptors.
  • Formerly EC 1.2.2.3.
 4 A0A0E0T5B3 A0A0E0T5B3 Q727P3 Q727P3
Formate dehydrogenase. [EC: 1.17.1.9]
Formate + NAD(+) = CO(2) + NADH.
  • The enzyme from most aerobic organisms is devoid of redox-active centers but that from the proteobacterium Methylosinus trichosporium contains iron-sulfur centers, flavin and a molybdenum center.
  • Together with EC 1.12.1.2, forms a system previously known as formate hydrogenlyase.
  • Formerly EC 1.2.1.2.
 1 P46448