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CATH Superfamily 1.10.1070.11

Phosphatidylinositol 3-/4-kinase, 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:

"
Phosphatidylinositol 3-/4-kinase, 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 1656: Phosphotidylinositol kinase Tel1, putative

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
Non-specific serine/threonine protein kinase. [EC: 2.7.11.1]
ATP + a protein = ADP + a phosphoprotein.
  • This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date.
  • Formerly EC 2.7.1.37 and EC 2.7.1.70.
 41 A0A024R3C7 A0A061I4Z2 A0A074TTN0 A0A086KQ69 A0A086LBU5 A0A086M683 A0A086QTR1 A0A0B0EBB5 A0A0B2RGH0 A0A0B7FZI2
(31 more...)
Phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). [EC: 5.4.2.11]
2-phospho-D-glycerate = 3-phospho-D-glycerate.
  • The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor.
  • The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His(10) in man and Escherichia coli, His(8) in Saccharomyces cerevisiae).
  • This phosphate can be transferred to the free OH of 2-phospho-D- glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine.
  • Cf. EC 5.4.2.12.
  • The enzyme has no requirement for metal ions.
  • This enzyme also catalyze, slowly, the reactions of EC 5.4.2.4.
  • Formerly EC 2.7.5.3 and EC 5.4.2.1.
 5 A0A1D6MNJ8 A0A1D6MNK5 A0A1D6MNK6 A0A1D6MNK7 A0A1D6MNK8
Phosphatidylinositol 3-kinase. [EC: 2.7.1.137]
ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo- inositol 3-phosphate.
    		 1 A3LT76
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