 |
|
| PROSITE documentation PDOC00519 |
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) |
| Consensus pattern: |
[LIVMFYWCS]-[LIVMFYWCAH]-x-D-[ED]-[IVA]-x(2,3)-[GAT]-[LIVMFAGCYN]-x(0,1)-[RSACLIH]-x-[GSADEHRM]-x(10,16)-[DH]-[LIVMFCAG]-[LIVMFYSTAR]-x(2)-[GSA]-K-x(2,3)-[GSTADNV]-[GSAC]
K is the pyridoxal-P attachment site |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE |
|
|
|
| Matching PDB structures:
1D7R 1D7S 1D7U 1D7V ... [ALL] |
References:
| 1 |
Authors | Bairoch A. |
| Source | Unpublished observations (1992). |
| 2 |
Authors | Yonaha K., Nishie M., Aibara S. |
| Source | J. Biol. Chem. 267:12506-12510(1992). |
Copyright:
PROSITE is copyright. It is produced by the Swiss Institute of
Bioinformatics (SIB). 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 license@isb-sib.ch or
see: http://www.expasy.org/prosite/prosite_license.htm.
Miscellaneous:
View entry in original PROSITE document format
View entry in raw text format (no links)