To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https
PROSITE documentation PDOC00519 [for PROSITE entry PS00600]

Aminotransferases class-III pyridoxal-phosphate attachment site





Description

Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped [1,2] into subfamilies. One of these, called class-III, currently consists of the following enzymes:

  • Acetylornithine aminotransferase (EC 2.6.1.11) which catalyzes the transfer of an amino group from acetylornithine to α-ketoglutarate, yielding N-acetyl-glutamic-5-semi-aldehyde and glutamic acid.
  • Ornithine aminotransferase (EC 2.6.1.13), which catalyzes the transfer of an amino group from ornithine to α-ketoglutarate, yielding glutamic-5- semi-aldehyde and glutamic acid.
  • Omega-amino acid--pyruvate aminotransferase (EC 2.6.1.18), which catalyzes transamination between a variety of omega-amino acids, mono- and diamines, and pyruvate. It plays a pivotal role in omega amino acids metabolism.
  • 4-aminobutyrate aminotransferase (EC 2.6.1.19) (GABA transaminase), which catalyzes the transfer of an amino group from GABA to α-ketoglutarate, yielding succinate semialdehyde and glutamic acid.
  • DAPA aminotransferase (EC 2.6.1.62), a bacterial enzyme (gene bioA) which catalyzes an intermediate step in the biosynthesis of biotin, the transamination of 7-keto-8-aminopelargonic acid (7-KAP) to form 7,8- diaminopelargonic acid (DAPA).
  • 2,2-dialkylglycine decarboxylase (EC 4.1.1.64), a Pseudomonas cepacia enzyme (gene dgdA) that catalyzes the decarboxylating amino transfer of 2,2-dialkylglycine and pyruvate to dialkyl ketone, alanine and carbon dioxide.
  • Glutamate-1-semialdehyde aminotransferase (EC 5.4.3.8) (GSA). GSA is the enzyme involved in the second step of porphyrin biosynthesis, via the C5 pathway. It transfers the amino group on carbon 2 of glutamate-1- semialdehyde to the neighbouring carbon, to give delta-aminolevulinic acid.
  • Bacillus subtilis aminotransferase yhxA.
  • Bacillus subtilis aminotransferase yodT.
  • Haemophilus influenzae aminotransferase HI0949.
  • Caenorhabditis elegans aminotransferase T01B11.2.

The sequence around the pyridoxal-phosphate attachment site of this class of enzyme is sufficiently conserved to allow the creation of a specific pattern.

Last update:

December 2004 / Pattern and text revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

AA_TRANSFER_CLASS_3, PS00600; Aminotransferases class-III pyridoxal-phosphate attachment site  (PATTERN)


References

1AuthorsBairoch A.
SourceUnpublished observations (1992).

2AuthorsYonaha K., Nishie M., Aibara S.
SourceJ. Biol. Chem. 267:12506-12510(1992).



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)