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CATH Superfamily 3.40.1190.10

Mur-like, catalytic 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:

"
Mur-like, catalytic 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 11515: Cyanophycin synthetase

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
Cyanophycin synthase (L-aspartate-adding). [EC: 6.3.2.29]
ATP + (L-Asp(4-L-Arg))(n) + L-Asp = ADP + phosphate + (L-Asp(4-L- Arg))(n)-L-Asp.
  • Both this enzyme and EC 6.3.2.30 are required for the elongation of cyanophycin, which is a protein-like cell inclusion that is unique to cyanobacteria and acts as a temporary nitrogen store.
  • Both enzymes are found in the same protein but have different active sites.
  • Both L-Asp and L-Arg must be present before either enzyme will display significant activity.
 18 A0A068N621 G5J5X1 G6FRG6 K7VWY7 K9PFK1 K9QHB2 K9ZFT6 O86109 P56947 P58572
(8 more...)
Cyanophycin synthase (L-arginine-adding). [EC: 6.3.2.30]
ATP + (L-Asp(4-L-Arg))(n)-L-Asp + L-Arg = ADP + phosphate + (L-Asp(4-L- Arg))(n+1).
  • Both this enzyme and EC 6.3.2.29 are required for the elongation of cyanophycin, which is a protein-like cell inclusion that is unique to cyanobacteria and acts as a temporary nitrogen store.
  • Both enzymes are found in the same protein but have different active sites.
  • Both L-Asp and L-Arg must be present before either enzyme will display significant activity.
  • Canavanine and lysine can be incoporated into the polymer instead of arginine.
 8 G5J5X1 O86109 P56947 P58572 P73833 Q9KGY4 T2IT86 W6FL80
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase. [EC: 6.3.2.13]
ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6- diaminoheptanedioate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L- alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate.
  • Involved in the synthesis of a cell-wall peptide.
  • This enzyme adds diaminopimelate in Gram-negative organisms and in some Gram-positive organisms; in others EC 6.3.2.7 adds lysine instead.
  • It is the amino group of the L-center of the diaminopimelate that is acylated.
 1 B2JA46
D-alanine--D-alanine ligase. [EC: 6.3.2.4]
ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine.
  • Involved with EC 6.3.2.7 or EC 6.3.2.13, EC 6.3.2.8, EC 6.3.2.9 and EC 6.3.2.10 in the synthesis of a cell-wall peptide.
 1 B2JA46
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