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CATH Superfamily 3.40.50.300

P-loop containing nucleotide triphosphate hydrolases

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:

"
P-loop containing nucleotide triphosphate hydrolases
".

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 633516: UPF0200 protein VNG_2452C

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
Dephospho-CoA kinase. [EC: 2.7.1.24]
ATP + 3'-dephospho-CoA = ADP + CoA.
    		 17 A0A0E3SPA5 A0A0F7PG57 A0A0N9N822 A0A0W8FGR1 A0A151ACH2 A0A166EZQ4 D3SUW5 D4GYX4 G0LMJ8 L5N271
    (7 more...)
    Adenylate kinase. [EC: 2.7.4.3]
    ATP + AMP = 2 ADP.
    • Inorganic triphosphate can also act as donor.
    		 2 A0A166CM80 Q6L0V8
    (d)CMP kinase. [EC: 2.7.4.25]
    ATP + (d)CMP = ADP + (d)CDP.
    • The prokaryotic cytidine monophosphate kinase specifically phosphorylates CMP (or dCMP), using ATP as the preferred phosphoryl donor.
    • Unlike EC 2.7.4.14, a eukaryotic enzyme that phosphorylates UMP and CMP with similar efficiency, the prokaryotic enzyme phosphorylates UMP with very low rates, and this function is catalyzed in prokaryotes by EC 2.7.4.22.
    • The enzyme phosphorylates dCMP nearly as well as it does CMP.
    		 2 A0A165YWK2 A0A166DFH5
    Sulfate adenylyltransferase. [EC: 2.7.7.4]
    ATP + sulfate = diphosphate + adenylyl sulfate.
    • The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme: ATP sulfurylase, which catalyzes the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate and the second step is catalyzed by the APS kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme bound APS and ATP.
    • This is in contrast to what is found in bacteria, yeasts, fungi and plants, where the formation of PAPS is carried out by two individual polypeptides, EC 2.7.7.4 and EC 2.7.1.25.
    		 1 U2F745
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