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:

"
Aspartate Aminotransferase, domain 1
".

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 40: Tyrosine aminotransferase

There are 3 EC terms in this cluster

Please note: EC 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.

Note: 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.

EC Term Annotations Evidence
Tyrosine transaminase. [EC: 2.6.1.5]
L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate.
  • L-phenylalanine can act instead of L-tyrosine.
  • The mitochondrial enzyme may be identical with EC 2.6.1.1.
  • The three isoenzymic forms are interconverted by EC 3.4.22.32 and EC 3.4.22.33.
  • The enzyme can also catalyze the final step in the methionine-salvage pathway of Klebsiella pneumoniae.
12 A0A140VKB7 A0A140VKB7 A0A178UPS5 A0A178UPS5 P04694 P17735 P17735 Q54K95 Q58CZ9 Q8QZR1
(2 more...)
Nicotianamine aminotransferase. [EC: 2.6.1.80]
Nicotianamine + 2-oxoglutarate = 3''-deamino-3''-oxonicotianamine + L-glutamate.
  • This enzyme is produced by grasses.
  • They secrete both the nicotianamine and the transaminated product into the soil around them.
  • Both compounds chelate Fe(2+) and Fe(3+); these chelators, called mugineic acid family phytosiderophores, are taken up by the grass, which is thereby supplied with iron.
2 Q9ST02 Q9ST03
L-cystine beta-lyase. [EC: 4.4.1.35]
L-cystine + H(2)O = L-thiocysteine + pyruvate + NH(3).
  • The enzyme cleaves a carbon-sulfur bond, releasing L-thiocysteine and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia.
  • The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10.
  • The enzyme from Brassica oleracea var. italica (broccoli) does not act on cysteine or cystathionine.
1 Q9SUR6