Protein Family Models

This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model. (from Pfam)

Date:

2024-08-14

This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4, Swiss:P00561. Acetylglutamate kinase EC:2.7.2.8, Swiss:Q07905. Glutamate 5-kinase EC:2.7.2.11, Swiss:P07005. Uridylate kinase EC:2.7.4.-, Swiss:P29464. Carbamate kinase EC:2.7.2.2, Swiss:O96432. [1]. 10860751. The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight in. Ramon-Maiques S, Marina A, Uriarte M, Fita I, Rubio V;. J Mol Biol 2000;299:463-476. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

bifunctional aspartate kinase/homoserine dehydrogenase II catalyzes the phosphorylation of L-aspartate to 4-phospho-L-aspartate and the conversion of L-homoserine to L-aspartate-4-semialdehyde, the first and third steps of the aspartate pathway

Date:

2017-07-10

Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys (and its precursor diaminopimelate), Met, and Thr. Prokaryotic genomes frequently encode multiple aspartate kinases. 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.

Date:

2024-05-30

Catalyzes the phosphorylation of aspartate to form aspartyl-4-phosphate as well as conversion of aspartate semialdehyde to homoserine; functions in a number of amino acid biosynthetic pathways

Gene:

metL

Date:

2020-10-26