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:
"D-serine dehydratase-like domain
".
FunFam 6: D-threo-3-hydroxyaspartate 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 3 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 |
|---|---|---|
|
D-serine ammonia-lyase activity GO:0008721
Catalysis of the reaction: D-serine = pyruvate + NH3.
|
1 | Q54XE5 (/IDA) |
|
Ammonia-lyase activity GO:0016841
Catalysis of the release of ammonia by the cleavage of a carbon-nitrogen bond or the reverse reaction with ammonia as a substrate.
|
1 | B2DFG5 (/IDA) |
|
Pyridoxal phosphate binding GO:0030170
Interacting selectively and non-covalently with pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
|
1 | B2DFG5 (/IMP) |
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 |
|---|---|---|
|
D-serine catabolic process GO:0036088
The chemical reactions and pathways resulting in the breakdown of D-serine, the D-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid.
|
1 | Q54XE5 (/IDA) |
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.
