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CATH Superfamily 3.30.450.20

PAS 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: 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 21582: Probable diguanylate cyclase YegE

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
Cyclic-guanylate-specific phosphodiesterase. [EC: 3.1.4.52]
Cyclic di-3',5'-guanylate + H(2)O = 5'-phosphoguanylyl(3'->5')guanosine.
  • Inhibited by Ca(2+) and Zn(2+).
  • Linearizes cyclic di-3',5'-guanylate, the product of EC 2.7.7.65 and an allosteric activator of EC 2.4.1.12 rendering it inactive.
  • It is the balance between these two enzymes that determines the cellular level of cyclic di-3',5'-guanylate.
 20 A0A023Z060 A0A025CBT9 A0A094XXS4 A0A0A1ABV0 A0A0F3UA25 A0A0I1BDR0 A0A0K3EVD3 A0A0K3ZQ66 A0A0K5FBF8 A0A0K6CVW4
(10 more...)
Diguanylate cyclase. [EC: 2.7.7.65]
2 GTP = 2 diphosphate + cyclic di-3',5'-guanylate.
  • Can be activated by BeF3, a phosphoryl mimic, which results in dimerization.
  • Dimerization is required but is not sufficient for diguanylate- cyclase activity.
  • Cyclic di-3',5'-guanylate is an intracellular signaling molecule that controls motility and adhesion in bacterial cells; it was first identified as having a positive allosteric effect on EC 2.4.1.12.
 5 A0A094XXS4 A0A1J0HCU0 E3PCL5 L2UXN9 P38097
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