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:
"Fumarase/aspartase (Central domain)
".
FunFam 12: Tyrosine ammonia-lyase
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 6 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 |
|---|---|---|
|
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.
|
4 | B8ZV93 (/IDA) B8ZV94 (/IDA) Q0VZ68 (/IDA) Q0VZ68 (/IDA) |
|
Tyrosine 2,3-aminomutase activity GO:0050368
Catalysis of the reaction: L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate.
|
4 | B8ZV93 (/IDA) B8ZV94 (/IDA) Q0VZ68 (/IDA) Q0VZ68 (/IDA) |
|
Phenylalanine ammonia-lyase activity GO:0045548
Catalysis of the reaction: L-phenylalanine = NH(4)(+) + trans-cinnamate.
|
3 | B2J528 (/IDA) Q3M5Z3 (/IDA) Q3M5Z3 (/IDA) |
|
Histidine ammonia-lyase activity GO:0004397
Catalysis of the reaction: L-histidine = urocanate + NH3.
|
2 | Q87V42 (/ISS) Q87V42 (/ISS) |
|
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
1 | Q3IWB0 (/IPI) |
|
Tyrosine ammonia-lyase activity GO:0052883
Catalysis of the reaction: L-tyrosine = NH(4)(+) + trans-4-coumarate.
|
1 | Q3IWB0 (/IDA) |
There are 7 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 |
|---|---|---|
|
Toxin biosynthetic process GO:0009403
The chemical reactions and pathways resulting in the formation of toxin, a poisonous compound (typically a protein) that is produced by cells or organisms and that can cause disease when introduced into the body or tissues of an organism.
|
4 | B8ZV93 (/IDA) B8ZV94 (/IDA) Q0VZ68 (/IDA) Q0VZ68 (/IDA) |
|
Phenylpropanoid biosynthetic process GO:0009699
The chemical reactions and pathways resulting in the formation of aromatic derivatives of trans-cinnamic acid.
|
4 | B2J528 (/IDA) Q3IWB0 (/IDA) Q3M5Z3 (/IDA) Q3M5Z3 (/IDA) |
|
Protein homotetramerization GO:0051289
The formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits.
|
4 | B2J528 (/IDA) Q3IWB0 (/IDA) Q3M5Z3 (/IDA) Q3M5Z3 (/IDA) |
|
Aromatic amino acid family metabolic process GO:0009072
The chemical reactions and pathways involving aromatic amino acid family, amino acids with aromatic ring (phenylalanine, tyrosine, tryptophan).
|
3 | B2J528 (/IDA) Q3M5Z3 (/IDA) Q3M5Z3 (/IDA) |
|
Cinnamic acid biosynthetic process GO:0009800
The chemical reactions and pathways resulting in the formation of cinnamic acid, 3-phenyl-2-propenoic acid.
|
3 | B2J528 (/IDA) Q3M5Z3 (/IDA) Q3M5Z3 (/IDA) |
|
Cellular amino acid metabolic process GO:0006520
The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups, as carried out by individual cells.
|
2 | Q87V42 (/ISS) Q87V42 (/ISS) |
|
Tyrosine catabolic process GO:0006572
The chemical reactions and pathways resulting in the breakdown of tyrosine, an aromatic amino acid, 2-amino-3-(4-hydroxyphenyl)propanoic acid.
|
1 | Q3IWB0 (/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.
