Family T5
Summary for family T5
| Family type peptidase | T05.001 - ornithine acetyltransferase precursor (Saccharomyces cerevisiae), MEROPS Accession MER0011829 (peptidase unit: 215-441) |
| Content of family | Peptidase family T5 contains the self-processing ornithine acetyltransferase precursor. |
| History |
Identifier created: MEROPS 6.4 (24 September 2003)
|
| Catalytic type | Threonine |
| Active site residues | T215 |
| Active site | Maturation of the precursor occurs through autoproteolysis of Ala214 Thr215. The mature product produced is a 57kDa heterodimer with subunits of 31kDa and 26kDa. Mutation of the catalytic threonine renders the peptidase catalytically inactive (Abadjieva et al., 2000). |
| Activities and specificities | The region around the scissile bond of the precursor protein is highly conserved. In the type example for family T5 the sequence is KGAGMICPNMATLLG. The mutation of the threonine immediately C-terminal to the scissile bond to an alanine results in the accumulation of the uncleaved precursor (Abadjieva et al., 2000) |
| Molecular structure | The tertiary structure has been solved for the homologue from Streptomyces clavuligerus, and shows an alpha/beta/beta/alpha fold similar to that of other Ntn-hydrolases. However, differences in the connectivity imply a different structural fold derived from convergent evolution, and the only true structural homologue is the DmpA aminopeptidase (P01.001) (Elkins et al., 2005). Because of the structural relationship to members of family P1, T5 is included in the same clan, PE. |
| Clan | PE |
