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CATH Superfamily 3.30.470.20

ATP-grasp fold, B domain

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:

"
ATP-grasp fold, B domain
".

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 7860: ATP-grasp protein

There are 1 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-aspartate ligase. [EC: 6.3.1.12]
ATP + D-aspartate + (beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L- Lys-D-Ala-D-Ala))(n) = (beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu- 6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala))(n) + ADP + phosphate.
  • Forms part of the peptidoglycan assembly pathway of Gram-positive bacteria grown in medium containing D-Asp.
  • Normally, the side chains the acylate the 6-amino group of the L-lysine residue contain L-Ala-L-Ala but these amino acids are replaced by D-Asp when D-Asp is included in the medium.
  • Hybrid chains containing L-Ala-D-Asp, L-Ala-L-Ala-D-Asp or D-Asp-L- Ala are not formed.
  • Highly specific for D-aspartate, as L-aspartate, D-glutamate, D-alanine, D-iso-asparagine and D-malic acid are not substrates.
  • In Enterococcus faecium, the substrate D-aspartate is produced by EC 5.1.1.13.
 17 A0A0M1XC66 A0A0M1Y0R8 A0A0M1ZTU3 A0A0M2A1D3 A0A0M2AL54 A0A0M2AYR6 A0A133CK82 C9B4Y5 C9BY27 D4REQ7
(7 more...)
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