View in Gene3D

CATH Superfamily 3.90.1150.10

Aspartate Aminotransferase, 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:

"
Aspartate Aminotransferase, 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.
« Back to all FunFams

FunFam 12222: Cystathionine gamma-synthase, PLP-dependent

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
Cystathionine gamma-synthase. [EC: 2.5.1.48]
O(4)-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate.
  • Also reacts with H(2)S and methanethiol as replacing agents, producing homocysteine and methionine, respectively.
  • In the absence of thiol, can also catalyze beta,gamma-elimination to form 2-oxobutanoate, succinate and ammonia.
  • Formerly EC 4.2.99.9.
 946 A0A017I4J6 A0A017I4J6 A0A023V5H2 A0A023V5H2 A0A023Z6M9 A0A023Z6M9 A0A024KKQ1 A0A024KKQ1 A0A025C1K1 A0A025C1K1
(936 more...)
Cystathionine gamma-lyase. [EC: 4.4.1.1]
L-cystathionine + H(2)O = L-cysteine + NH(3) + 2-oxobutanoate.
  • The enzyme cleaves a carbon-sulfur bond, releasing L-cysteine and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia.
  • The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10.
  • Also catalyzes the conversion of L-homoserine to 2-oxobutanoate and ammonia, of L-cystine to thiocysteine, pyruvate and ammonia, and of L-cysteine to pyruvate, hydrogen sulfide and ammonia.
  • Formerly EC 4.2.1.15.
 30 A0A0J6DGV9 A0A0J6DGV9 A0A1C3A089 A0A1C3A089 A0A1J7PCG2 A0A1J7PCG2 A0A1L3UNQ6 A0A1L3UNQ6 A0A1L6MFR6 A0A1L6MFR6
(20 more...)
Cystathionine beta-lyase. [EC: 4.4.1.8]
L-cystathionine + H(2)O = L-homocysteine + NH(3) + pyruvate.
  • The enzyme cleaves a carbon-sulfur bond, releasing L-homocysteine 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.
  • The enzyme from some sources also acts on L-cystine, forming pyruvate, ammonia and cysteine persulfide, and a number of related compounds.
  • Possibly identical, in Saccharomyces cerevisiae, with EC 4.4.1.6.
 2 F5RR55 F5RR55
CATH-Gene3D is a Global Biodata Core Resource Learn more...