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CATH Superfamily 3.30.1060.10

Peptide methionine sulphoxide reductase MsrA

The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was named:

"
Peptide methionine sulphoxide reductase MsrA
".

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 3: Peptide methionine sulfoxide reductase MsrA

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
Peptide-methionine (S)-S-oxide reductase. [EC: 1.8.4.11]
(1) Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L- methionine (S)-S-oxide + thioredoxin. (2) L-methionine + thioredoxin disulfide + H(2)O = L-methionine (S)-S- oxide + thioredoxin.
  • The reaction occurs in the reverse direction to that shown above.
  • Exhibits high specificity for the reduction of the S-form of L-methionine S-oxide, acting faster on the residue in a peptide than on the free amino acid.
  • On the free amino acid, it can also reduce D-methionine (S)-S-oxide but more slowly.
  • Plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged.
  • The reaction proceeds via a sulfenic-acid intermediate.
  • Formerly EC 1.8.4.6.
 416 A0A0D1K117 A0A0D1K117 A0A0D1K117 A0A0D1K117 A0A0D1K117 A0A0D1K117 A0A0D1K117 A0A0D1K117 A0A0D1K117 A0A0D1K117
(406 more...)
Peptide-methionine (R)-S-oxide reductase. [EC: 1.8.4.12]
Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L- methionine (R)-S-oxide + thioredoxin.
  • The reaction occurs in the reverse direction to that shown above.
  • Exhibits high specificity for reduction of the R-form of methionine S-oxide, with higher activity being observed with L-methionine S-oxide than with D-methionine S-oxide.
  • While both free and protein-bound methionine (R)-S-oxide act as substrates, the activity with the peptide-bound form is far greater.
  • Plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged.
  • The reaction proceeds via a sulfenic-acid intermediate.
  • For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but thionein works well.
 9 A0A0H6EDV0 A0A0H6EDV0 A0A0H6EDV0 A0A0K9UQ55 A0A0K9UQ55 A0A0K9UQ55 Q9KLX6 Q9KLX6 Q9KLX6
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