CATH Superfamily 2.40.40.20
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: waiting to be named.
FunFam 9: 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 10 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 |
|---|---|---|
|
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
|
12 |
P33225 (/IPI)
P33225 (/IPI)
P33225 (/IPI)
P33225 (/IPI)
P33225 (/IPI)
P33225 (/IPI)
P33225 (/IPI)
P33225 (/IPI)
P33225 (/IPI)
P33225 (/IPI)
(2 more) |
|
Molybdenum ion binding GO:0030151
Interacting selectively and non-covalently with molybdenum (Mo) ions.
|
12 |
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
(2 more) |
|
Cofactor binding GO:0048037
Interacting selectively and non-covalently with a cofactor, a substance that is required for the activity of an enzyme or other protein. Cofactors may be inorganic, such as the metal atoms zinc, iron, and copper in certain forms, or organic, in which case they are referred to as coenzymes. Cofactors may either be bound tightly to active sites or bind loosely with the substrate.
|
12 |
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
(2 more) |
|
Cofactor binding GO:0048037
Interacting selectively and non-covalently with a cofactor, a substance that is required for the activity of an enzyme or other protein. Cofactors may be inorganic, such as the metal atoms zinc, iron, and copper in certain forms, or organic, in which case they are referred to as coenzymes. Cofactors may either be bound tightly to active sites or bind loosely with the substrate.
|
12 |
P33225 (/ISM)
P33225 (/ISM)
P33225 (/ISM)
P33225 (/ISM)
P33225 (/ISM)
P33225 (/ISM)
P33225 (/ISM)
P33225 (/ISM)
P33225 (/ISM)
P33225 (/ISM)
(2 more) |
|
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+.
|
12 |
P33225 (/IMP)
P33225 (/IMP)
P33225 (/IMP)
P33225 (/IMP)
P33225 (/IMP)
P33225 (/IMP)
P33225 (/IMP)
P33225 (/IMP)
P33225 (/IMP)
P33225 (/IMP)
(2 more) |
|
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) |
|
Trimethylamine-N-oxide reductase activity GO:0009033
Catalysis of the reaction: NADH + H+ + trimethylamine-N-oxide = NAD+ + trimethylamine + H2O.
|
7 | Q8EHI9 (/ISS) Q9KRF0 (/ISS) Q9KRF0 (/ISS) Q9KRF0 (/ISS) Q9KRF0 (/ISS) Q9KRF0 (/ISS) Q9KRF0 (/ISS) |
|
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 4 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 |
|---|---|---|
|
Aerobic respiration GO:0009060
The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which requires oxygen as the terminal electron acceptor.
|
12 |
P33225 (/IEP)
P33225 (/IEP)
P33225 (/IEP)
P33225 (/IEP)
P33225 (/IEP)
P33225 (/IEP)
P33225 (/IEP)
P33225 (/IEP)
P33225 (/IEP)
P33225 (/IEP)
(2 more) |
|
Anaerobic respiration GO:0009061
The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which uses compounds other than oxygen (e.g. nitrate, sulfate) as the terminal electron acceptor.
|
12 |
P33225 (/IEP)
P33225 (/IEP)
P33225 (/IEP)
P33225 (/IEP)
P33225 (/IEP)
P33225 (/IEP)
P33225 (/IEP)
P33225 (/IEP)
P33225 (/IEP)
P33225 (/IEP)
(2 more) |
|
Anaerobic respiration GO:0009061
The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which uses compounds other than oxygen (e.g. nitrate, sulfate) as the terminal electron acceptor.
|
7 | Q8EHI9 (/ISS) Q9KRF0 (/ISS) Q9KRF0 (/ISS) Q9KRF0 (/ISS) Q9KRF0 (/ISS) Q9KRF0 (/ISS) Q9KRF0 (/ISS) |
|
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 3 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.
|
14 |
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
P33225 (/IDA)
(4 more) |
|
Cell wall GO:0005618
The rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal, most prokaryotic cells and some protozoan parasites, maintaining their shape and protecting them from osmotic lysis. In plants it is made of cellulose and, often, lignin; in fungi it is composed largely of polysaccharides; in bacteria it is composed of peptidoglycan; in protozoan parasites such as Giardia species, it's made of carbohydrates and proteins.
|
8 | O06817 (/HDA) O06817 (/HDA) O06817 (/HDA) O06817 (/HDA) O06817 (/HDA) O06817 (/HDA) O06817 (/HDA) O06817 (/HDA) |
|
Trimethylamine-N-oxide reductase complex GO:0009322
An enzyme complex that catalyzes the reduction of trimethylamine N-oxide to trimethylamine.
|
7 | Q8EHI9 (/ISS) Q9KRF0 (/ISS) Q9KRF0 (/ISS) Q9KRF0 (/ISS) Q9KRF0 (/ISS) Q9KRF0 (/ISS) Q9KRF0 (/ISS) |
