View in Gene3D

CATH Superfamily 3.40.50.1100

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.
« Back to all FunFams

FunFam 25339: 1-aminocyclopropane-1-carboxylate deaminase, putat...

There are 4 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
1-aminocyclopropane-1-carboxylate deaminase. [EC: 3.5.99.7]
1-aminocyclopropane-1-carboxylate + H(2)O = 2-oxobutanoate + NH(3).
  • The enzyme, found in certain soil bacteria and fungi, catalyzes the ring opening of 1-aminocyclopropane-1-carboxylate, the immediate precursor to ethylene, an important plant hormone that regulates fruit ripening and other processes.
  • The enzyme releases an unstable enamine product that tautomerizes to an imine form, which undergoes spontaneous hydrolytic deamination.
  • The enzyme has been used to make fruit ripening dependent on externally added ethylene, as it removes the substrate for endogenous ethylene formation.
  • Formerly EC 4.1.99.4.
 1123 A0A011USP6 A0A014KZR2 A0A014LFL8 A0A017HT34 A0A022GGF8 A0A023XVF0 A0A038H4H2 A0A060I7W9 A0A060PHY8 A0A061MRK4
(1113 more...)
D-cysteine desulfhydrase. [EC: 4.4.1.15]
D-cysteine + H(2)O = H(2)S + NH(3) + pyruvate.
    		 998 A0A010RQ82 A0A017IEQ0 A0A023P972 A0A023VEP6 A0A023YYF0 A0A024HE74 A0A024KW10 A0A024L1L0 A0A025C2D2 A0A026REQ5
    (988 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.
    		 26 A0A0A3FKL4 A0A0H4REY0 A0A0K6LHG1 A0A0K6N3L7 A0A0L6CUK9 A0A0M6Z1M2 A0A0M6ZPD7 A0A0M7AQA8 A0A0P1E5E7 A0A0P1ELR4
    (16 more...)
    Sulfopyruvate decarboxylase. [EC: 4.1.1.79]
    3-sulfopyruvate = 2-sulfoacetaldehyde + CO(2).
    • Does not decarboxylate pyruvate or phosphonopyruvate.
    • The enzyme appears to be oxygen-sensitive.
    		 1 F7ZKV6