PROSITE documentation PDOC00847Aspartate-semialdehyde dehydrogenase signature
Aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) (ASD) catalyzes the second step in the common biosynthetic pathway leading from Asp to diaminopimelate and Lys, to Met, and to Thr; the NADP-dependent reductive dephosphorylation of L-aspartyl phosphate to L-aspartate-semialdehyde. In bacteria and fungi, ASD is a protein of about 40 Kd (340 to 370 residues) whose sequence is not extremely well conserved [1]. A conserved cysteine residue has been implicated as important for the catalytic activity [2].
The region of conservation around the active site residue is too small to be used as as signature pattern. We have used another more conserved region, located in the last third of the sequence, and which contains both a conserved cysteine as well as an histidine.
Last update:November 1995 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Baril C. Richaud C. Fournie E. Baranton G. Saint Girons I. |
| Title | Cloning of dapD, aroD and asd of Leptospira interrogans serovar icterohaemorrhagiae, and nucleotide sequence of the asd gene. | |
| Source | J. Gen. Microbiol. 138:47-53(1992). | |
| PubMed ID | 1348268 |
| 2 | Authors | Karsten W.E. Viola R.E. |
| Title | Identification of an essential cysteine in the reaction catalyzed by aspartate-beta-semialdehyde dehydrogenase from Escherichia coli. | |
| Source | Biochim. Biophys. Acta 1121:234-238(1992). | |
| PubMed ID | 1350921 |
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