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:
"Enolase-like C-terminal domain
".
FunFam 5: Putative L-rhamnonate dehydratase
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 8 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 |
|---|---|---|
|
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
14 |
P77215 (/IDA)
P77215 (/IDA)
P77215 (/IDA)
P77215 (/IDA)
P77215 (/IDA)
P77215 (/IDA)
P77215 (/IDA)
P77215 (/IDA)
P77215 (/IDA)
P77215 (/IDA)
(4 more) |
|
L-rhamnonate dehydratase activity GO:0050032
Catalysis of the reaction: L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate + H(2)O.
|
14 |
P77215 (/IDA)
P77215 (/IDA)
P77215 (/IDA)
P77215 (/IDA)
P77215 (/IDA)
P77215 (/IDA)
P77215 (/IDA)
P77215 (/IDA)
P77215 (/IDA)
P77215 (/IDA)
(4 more) |
|
Mannonate dehydratase activity GO:0008927
Catalysis of the reaction: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H(2)O.
|
6 | A2R1E3 (/IDA) A2R1E3 (/IDA) A2R1E3 (/IDA) A2R1E3 (/IDA) A2R1E3 (/IDA) D9UNB2 (/IDA) |
|
Gluconate dehydratase activity GO:0047929
Catalysis of the reaction: D-gluconate = 2-dehydro-3-deoxy-D-gluconate + H(2)O.
|
5 | Q6L1T2 (/IDA) Q704D2 (/IDA) Q97U27 (/IDA) Q97U27 (/IDA) Q97U27 (/IDA) |
|
Galactonate dehydratase activity GO:0008869
Catalysis of the reaction: D-galactonate = 2-dehydro-3-deoxy-D-galactonate + H(2)O.
|
4 | Q6L1T2 (/IDA) Q97U27 (/IDA) Q97U27 (/IDA) Q97U27 (/IDA) |
|
Magnesium ion binding GO:0000287
Interacting selectively and non-covalently with magnesium (Mg) ions.
|
2 | B5GCP6 (/ISS) C7PW26 (/ISS) |
|
Magnesium ion binding GO:0000287
Interacting selectively and non-covalently with magnesium (Mg) ions.
|
1 | D9UNB2 (/IDA) |
|
Isomerase activity GO:0016853
Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.
|
1 | Q4KGI0 (/ISS) |
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 |
|---|---|---|
|
Cellular carbohydrate catabolic process GO:0044275
The chemical reactions and pathways resulting in the breakdown of carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y, as carried out by individual cells.
|
5 | A2R1E3 (/IDA) A2R1E3 (/IDA) A2R1E3 (/IDA) A2R1E3 (/IDA) A2R1E3 (/IDA) |
|
Carbohydrate metabolic process GO:0005975
The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. Includes the formation of carbohydrate derivatives by the addition of a carbohydrate residue to another molecule.
|
1 | Q704D2 (/IDA) |
|
Carbohydrate catabolic process GO:0016052
The chemical reactions and pathways resulting in the breakdown of carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
|
1 | D9UNB2 (/IDA) |
|
Aromatic compound catabolic process GO:0019439
The chemical reactions and pathways resulting in the breakdown of aromatic compounds, any substance containing an aromatic carbon ring.
|
1 | Q4KGI0 (/ISS) |
There are 0 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.