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CATH Superfamily 3.90.55.10

Dimethylsulfoxide Reductase, domain 3

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:

"
Dimethylsulfoxide Reductase, domain 3
".

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 1: Biotin sulfoxide reductase 2

Please note: GO 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.

There are 4 GO terms relating to "molecular function"

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.
GO Term Annotations Evidence
Molybdenum ion binding GO:0030151
Interacting selectively and non-covalently with molybdenum (Mo) ions.
 8 P20099 (/IMP) P20099 (/IMP) P20099 (/IMP) P20099 (/IMP) P20099 (/IMP) P20099 (/IMP) P20099 (/IMP) P20099 (/IMP)
L-methionine:thioredoxin-disulfide S-oxidoreductase activity GO:0033744
Catalysis of the reaction: L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.
 8 P20099 (/IDA) P20099 (/IDA) P20099 (/IDA) P20099 (/IDA) P20099 (/IDA) P20099 (/IDA) P20099 (/IDA) P20099 (/IDA)
Catalytic activity GO:0003824
Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
 6 Q9KQP8 (/ISS) Q9KQP8 (/ISS) Q9KQP8 (/ISS) Q9KQP8 (/ISS) Q9KQP8 (/ISS) Q9KQP8 (/ISS)
Trimethylamine-N-oxide reductase (cytochrome c) activity GO:0050626
Catalysis of the reaction: trimethylamine + 2 (ferricytochrome c)-subunit + H2O = trimethylamine-N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+.
 2 P46923 (/IDA) P46923 (/IDA)

There are 1 GO terms relating to "biological process"

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.
GO Term Annotations Evidence
Biotin biosynthetic process GO:0009102
The chemical reactions and pathways resulting in the formation of biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid.
 6 Q9KQP8 (/ISS) Q9KQP8 (/ISS) Q9KQP8 (/ISS) Q9KQP8 (/ISS) Q9KQP8 (/ISS) Q9KQP8 (/ISS)

There are 1 GO terms relating to "cellular component"

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.
GO Term Annotations Evidence
Outer membrane-bounded periplasmic space GO:0030288
The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.
 2 P46923 (/IDA) P46923 (/IDA)