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CATH Superfamily 3.10.196.10

Vitamin B12-dependent methionine synthase, activation domain

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:

"
Vitamin B12-dependent methionine synthase, activation 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 2: Methionine synthase

There are 1 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
Methionine synthase. [EC: 2.1.1.13]
5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine.
  • The enzyme becomes inactivated occasionally during its cycle by oxidation of Co(I) to Co(II).
  • Reactivation by reductive methylation is catalyzed by the enzyme itself, with S-adenosyl-L-methionine as the methyl donor and a reducing system.
  • For the mammalian enzyme, the reducing system involves NADPH and EC 1.16.1.8.
  • In bacteria, the reducing agent is flavodoxin, and no further catalyst is needed (the flavodoxin is kept in the reduced state by NADPH and EC 1.18.1.2).
  • Acts on the monoglutamate as well as the triglutamate folate, in contrast with EC 2.1.1.14, which acts only on the triglutamate.
 25 A0A045IUR4 A0A045IUR4 A0A045IUR4 A0A045IUR4 A0A045IUR4 A0A0H3LAV4 A0A0H3LAV4 A0A0H3LAV4 A0A0H3LAV4 A0A0H3LAV4
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