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:

"
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 9585: Citrate lyase subunit beta

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
Malyl-CoA lyase. [EC: 4.1.3.24]
(1) (S)-malyl-CoA = acetyl-CoA + glyoxylate. (2) (2R,3S)-2-methylmalyl-CoA = propanoyl-CoA + glyoxylate.
  • The enzyme from the bacterium Chloroflexus aurantiacus, which participates in the 3-hydroxypropanoate cycle for carbon assimilation, also has the activity of EC 4.1.3.25.
  • The enzymes from Rhodobacter species are part of acetate assimilation pathways.
  • The reactions are reversible.
15 A0A045K5Y1 A0A0G4DY62 A0A0H3M8P9 A0A0H3P5J9 A0A109S9M5 A0A109SQX4 A0A120J2P5 A0A1K3SM21 A0A1K6QWI9 A5U790
(5 more...)
Uroporphyrinogen-III C-methyltransferase. [EC: 2.1.1.107]
(1) S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L- homocysteine + precorrin-1. (2) S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2.
  • This enzyme catalyzes two sequential methylation reactions, the first forming precorrin-1 and the second leading to the formation of precorrin-2.
  • It is the first of three steps leading to the formation of siroheme from uroporphyrinogen III.
  • The second step involves an NAD(+)-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76) and the third step involves the chelation of Fe(2+) to sirohydrochlorin to form siroheme (EC 4.99.1.4).
  • In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p.
  • In some bacteria, steps 1-3 are catalyzed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirA being responsible for the above reaction.
  • Also involved in the biosynthesis of cobalamin.
5 A0A089QQB3 A0A0H3LHU9 A0A197IWC5 A0A1A9EBB3 A0A1L7MLU2
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