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CATH Superfamily 3.40.50.1100

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: 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 17: D-cysteine desulfhydrase

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
D-cysteine desulfhydrase. [EC: 4.4.1.15]
D-cysteine + H(2)O = H(2)S + NH(3) + pyruvate.
    		 6522 A0A023YYF0 A0A023YYF0 A0A023YYF0 A0A023YYF0 A0A023YYF0 A0A023YYF0 A0A023YYF0 A0A023YYF0 A0A023YYF0 A0A023YYF0
    (6512 more...)
    L-cysteate sulfo-lyase. [EC: 4.4.1.25]
    L-cysteate + H(2)O = hydrogensulfite + pyruvate + NH(3).
    • The enzyme cleaves a carbon-sulfur bond, releasing bisulfite and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia.
    • The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10.
    • D-cysteine can also act as a substrate, but more slowly.
    • It is converted into pyruvate, sulfide and ammonia.
    • The inducible enzyme from Silicibacter pomeroyi DSS-3 forms part of the cysteate-degradation pathway.
    		 1 Q5LL69