|PROSITE documentation PDOC00519
Aminotransferases class-III pyridoxal-phosphate attachment site
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 184.108.40.206) 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 220.127.116.11), 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 18.104.22.168), 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 22.214.171.124) (GABA transaminase), which
catalyzes the transfer of an amino group from GABA to α-ketoglutarate,
yielding succinate semialdehyde and glutamic acid.
- DAPA aminotransferase (EC 126.96.36.199), 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 188.8.131.52), a Pseudomonas cepacia
enzyme (gene dgdA) that catalyzes the decarboxylating amino transfer of
2,2-dialkylglycine and pyruvate to dialkyl ketone, alanine and carbon
- Glutamate-1-semialdehyde aminotransferase (EC 184.108.40.206) (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.
December 2004 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
|AA_TRANSFER_CLASS_3, PS00600; Aminotransferases class-III pyridoxal-phosphate attachment site (PATTERN)
K is the pyridoxal-P attachment site
|Sequences known to belong to this class detected by the pattern:
|Other sequence(s) detected in Swiss-Prot:
|Matching PDB structures:
1D7R 1D7S 1D7U 1D7V ... [ALL]
||Unpublished observations (1992).
||Yonaha K., Nishie M., Aibara S.
||J. Biol. Chem. 267:12506-12510(1992).
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