| Accession | TIGR00657 |
| Name | asp_kinases |
| Function | aspartate kinase |
| Trusted Cutoff | 208.70 |
| Domain Trusted Cutoff | 208.70 |
| Noise Cutoff | 91.15 |
| Domain Noise Cutoff | 91.15 |
| Isology Type | subfamily_domain |
| EC Number | 2.7.2.4 |
| HMM Length | 442 |
| Mainrole Category | Amino acid biosynthesis |
| Subrole Category | Aspartate family |
| Author | Haft DH |
| Entry Date | Dec 1 1999 10:45AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys (and its precursor diaminopimelate), Met, and Thr. In E. coli, a distinct isozyme is inhibited by each of the three amino acid products. The Met-sensitive (I) and Thr-sensitive (II) forms are bifunctional enzymes fused to homoserine dehydrogenases and form homotetramers, while the Lys-sensitive form (III) is a monofunctional homodimer.
The Lys-sensitive enzyme of Bacillus subtilis resembles the E. coli form but is an alpha 2/beta 2 heterotetramer, where the beta subunit is translated from an in-phase alternative initiator at Met-246. This may be a feature of a number of closely related forms, including a paralog from B. subtilis.
|
| References | SE
AL
A2 hmmalign
GA hmmsearch
DR EXPERIMENTAL; EGAD|9629|EC4024; monofunctional, Lys-sensitive homodimer
DR EXPERIMENTAL; EGAD|9487|EC0002; bifunctional, Thr-sensitive homotetramer
DR EXPERIMENTAL; EGAD|21696|EC3940; bifunctional, Met-sensistive homotetramer
DR EXPERIMENTAL; EGAD|52194|YER052C; mostly Thr-sensitive
DR EXPERIMENTAL; EGAD|75283|81007; bifunctional, chloroplast
|
| Genome Property | GenProp0160: aspartate semialdehyde biosynthesis from aspartate (HMM) |
