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CATH Superfamily 3.65.10.10

Enolpyruvate transferase 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:

"
Enolpyruvate transferase 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 8973: 3-phosphoshikimate 1-carboxyvinyltransferase 1, ch...

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
3-phosphoshikimate 1-carboxyvinyltransferase. [EC: 2.5.1.19]
Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O- (1-carboxyvinyl)-3-phosphoshikimate.
    		 2640 A0A010PFN9 A0A011LXA4 A0A011NI87 A0A011NL11 A0A011QIT4 A0A014LW13 A0A014Q6S5 A0A016XKY4 A0A017IG42 A0A022G031
    (2630 more...)
    UMP/CMP kinase. [EC: 2.7.4.14]
    (1) ATP + (d)CMP = ADP + (d)CDP. (2) ATP + UMP = ADP + UDP.
    • This eukaryotic enzyme is a bifunctional enzyme that catalyzes the phosphorylation of both CMP and UMP with similar efficiency.
    • dCMP can also act as acceptor.
    • Different from the monofunctional prokaryotic enzymes EC 2.7.4.25, CMP kinase and EC 2.7.4.22, UMP kinase.
    • This eukaryotic enzyme is a bifunctional enzyme that catalyzes the phosphorylation of both CMP and UMP with similar efficiency.
    • dCMP can also act as acceptor.
    • Different from the monofunctional prokaryotic enzymes EC 2.7.4.25 and EC 2.7.4.22.
    • Formerly EC 2.7.4.5.
    		 96 A0A014Q6S5 A0A016XKY4 A0A068YMW4 A0A077DDH3 A0A096FDH5 A0A096G1P8 A0A0A0DSZ2 A0A0C5J9R3 A0A0D0LG43 A0A0D7K8J2
    (86 more...)
    (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.
    		 3 A0A011R848 A0A1H5SAQ3 W7WF23
    Prephenate dehydrogenase. [EC: 1.3.1.12]
    Prephenate + NAD(+) = 4-hydroxyphenylpyruvate + CO(2) + NADH.
    • This enzyme in the enteric bacteria also possesses EC 5.4.99.5 activity and converts chorismate into prephenate.
    		 1 C9Y9W3