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CATH Superfamily 3.40.228.10

Dimethylsulfoxide Reductase, domain 2

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:

"
Dimethylsulfoxide Reductase, domain 2
".

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 5788: Trimethylamine-N-oxide reductase (Cytochrome c)

There are 5 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
Trimethylamine-N-oxide reductase (cytochrome c). [EC: 1.7.2.3]
Trimethylamine + 2 (ferricytochrome c)-subunit + H(2)O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H(+).
  • The cytochrome c involved in photosynthetic bacteria is a pentaheme protein.
  • The reductant is a membrane-bound multiheme cytochrome c.
  • Also reduces dimethyl sulfoxide to dimethyl sulfide.
 945 A0A017IF63 A0A017IG89 A0A024K928 A0A024KUM6 A0A024L2F1 A0A024L4G5 A0A027U5D6 A0A027U6T4 A0A028AUL2 A0A028AUU7
(935 more...)
Trimethylamine-N-oxide reductase. [EC: 1.6.6.9]
NADH + trimethylamine N-oxide = NAD(+) + trimethylamine + H(2)O.
    		 226 A0A023YVK7 A0A023YYB9 A0A024L2F1 A0A025CAX1 A0A025CR45 A0A027U5D6 A0A028AUU7 A0A028E0L8 A0A028E4M3 A0A029HX78
    (216 more...)
    Dimethylsulfoxide reductase. [EC: 1.8.5.3]
    Dimethylsulfide + menaquinone + H(2)O = dimethylsulfoxide + menaquinol.
    • Also reduces pyridine N-oxide and trimethylamine N-oxide, with lower activity, to the corresponding amines.
    		 32 A0A090RT70 A0A090SFQ2 A0A098BH84 A0A099UAY4 A0A0A1FTP0 A0A0A1RFN3 A0A0D6SDL0 A0A0G4JQ49 A0A0H2LSN2 A0A0H2M0Z7
    (22 more...)
    L-methionine (S)-S-oxide reductase. [EC: 1.8.4.13]
    L-methionine + thioredoxin disulfide + H(2)O = L-methionine (S)-S-oxide + thioredoxin.
    • The reaction occurs in the opposite direction to that given above.
    • Dithiothreitol can replace reduced thioredoxin.
    • L-methionine (R)-S-oxide is not a substrate (see EC 1.8.4.14).
    • Formerly EC 1.8.4.5.
    		 27 A0A070USH1 A0A090NES7 A0A090NF98 A0A0A6ZR95 A0A0E1C7E7 A0A0E1CLZ1 A0A0E1M4Q2 A0A0H3GLB2 A0A0J2EBN5 A0A0J2GBA8
    (17 more...)
    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.
    		 8 A0A090NES7 A0A0E1C7E7 A0A125XC51 A0A192CEW0 A0A193RSB6 E2XE77 W8UD73 W8ZYM6