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CATH Superfamily 1.10.439.10

Penicillin Amidohydrolase, domain 1

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 named:

"
Penicillin Amidohydrolase, 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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

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
Acyl-homoserine-lactone acylase. [EC: 3.5.1.97]
An N-acyl-L-homoserine lactone + H(2)O = L-homoserine lactone + a carboxylate.
  • Acyl-homoserine lactones (AHLs) are produced by a number of bacterial species and are used by them to regulate the expression of virulence genes in a process known as quorum-sensing.
  • Each bacterial cell has a basal level of AHL and, once the population density reaches a critical level, it triggers AHL-signaling which, in turn, initiates the expression of particular virulence genes.
  • Plants or animals capable of degrading AHLs would have a therapeutic advantage in avoiding bacterial infection as they could prevent AHL- signaling and the expression of virulence genes in quorum-sensing bacteria.
  • This quorum-quenching enzyme removes the fatty-acid side chain from the homoserine lactone ring of AHL-dependent quorum-sensing signal molecules.
  • It has broad specificity for AHLs with side changes ranging in length from 11 to 14 carbons.
  • Substituents at the 3'-position, as found in N-(3-oxododecanoyl)-L- homoserine lactone, do not affect this activity.
 35 A0A0M9HUU2 A0A0N0F4R0 A0A0N0W7T4 A0A0N0WIM7 A0A0P9QXR0 A0A0P9WH63 A0A0P9WHM5 A0A0Q0BU72 A0A0Q0CMD4 A0A1E3XY05
(25 more...)
Penicillin amidase. [EC: 3.5.1.11]
Penicillin + H(2)O = a carboxylate + 6-aminopenicillanate.
    		 18 A0A070FI48 A0A0H0R9W8 A0A3D1C3L2 A0A3W2RAS9 A0A402VCY5 B6I2M3 C8U0U0 D6I4I8 E0J480 F4VMW1
    (8 more...)
    Glutaryl-7-aminocephalosporanic-acid acylase. [EC: 3.5.1.93]
    (7R)-7-(4-carboxybutanamido)cephalosporanate + H(2)O = (7R)-7- aminocephalosporanate + glutarate.
    • Forms 7-aminocephalosporanic acid, a key intermediate in the synthesis of cephem antibiotics.
    • It reacts only weakly with cephalosporin C.
    		 2 P07662 Q9L5D6