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CATH Superfamily 3.30.70.360

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 19: Allantoate deiminase

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
Allantoate deiminase. [EC: 3.5.3.9]
Allantoate + H(2)O = (S)-ureidoglycine + NH(3) + CO(2).
  • This enzyme is part of the ureide pathway, which permits certain organisms to recycle the nitrogen in purine compounds.
  • This enzyme, which liberates ammonia from allantoate, is present in plants and bacteria.
  • In plants it is localized in the endoplasmic reticulum.
  • Requires manganese.
 5 A0A0E0Q1B9 A0A0E0Q1B9 O49434 Q655X8 Q655X8
N-carbamoyl-L-amino-acid hydrolase. [EC: 3.5.1.87]
N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H(2)O = L-2-amino acid + NH(3) + CO(2).
  • This enzyme, along with EC 3.5.1.77, EC 5.1.99.5 and EC 3.5.2.2, forms part of the reaction cascade known as the 'hydantoinase process', which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids.
  • The enzyme from Alcaligenes xylosoxidans has broad specificity for carbamoyl-L-amino acids, although it is inactive on the carbamoyl derivatives of glutamate, aspartate, arginine, tyrosine or tryptophan.
  • The enzyme from Sinorhizobium meliloti requires a divalent cation for activity and can hydrolyze N-carbamoyl-L-tryptophan as well as N-carbamoyl L-amino acids with aliphatic substituents.
  • The enzyme is inactive on derivatives of D-amino acids.
  • In addition to N-carbamoyl L-amino acids, the enzyme can also hydrolyze formyl and acetyl derivatives to varying degrees.
 1 Q01264