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:

"
Phosphoenolpyruvate-binding domains
".

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 9: 2-methylisocitrate lyase

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
Methylisocitrate lyase. [EC: 4.1.3.30]
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate.
  • Acts on threo-D(s)-2-methylisocitrate, but not on threo-D(s)- isocitrate, threo-DL-isocitrate or erythro-L(s)-isocitrate.
700 A0A070SMC2 A0A070SMC2 A0A070SMC2 A0A070SMC2 A0A070SMC2 A0A070SMC2 A0A070SMC2 A0A070SMC2 A0A070SMC2 A0A070SMC2
(690 more...)
Carboxyvinyl-carboxyphosphonate phosphorylmutase. [EC: 2.7.8.23]
1-carboxyvinyl carboxyphosphonate = 3-(hydrohydroxyphosphoryl)pyruvate + CO(2).
  • Catalyzes the transfer and decarboxylation of the carboxy(hydroxy)phosphoryl group, HOOC-P(O)(OH)- (phosphoryl being a 3-valent group), in the formation of an unusual C-P bond that is involved in the biosynthesis of the antibiotic bialaphos.
4 A0A178W7S1 A0A178W7S1 O49290 O49290