Protein Family Models

This entry represents the ACT domain, which is found twice in Aspartate kinase from Methanocaldococcus jannaschii, the enzyme that catalyses the phosphorylation of aspartic acid [6]. This domain folds as a four-stranded antiparallel sheet with two alpha-helices parallel to the sheet and located on one side of the sheet [1]. Paper describing PDB structure 2cdq. [1]. 16731588. A novel organization of ACT domains in allosteric enzymes revealed by the crystal structure of Arabidopsis aspartate kinase. Mas-Droux C, Curien G, Robert-Genthon M, Laurencin M, Ferrer JL, Dumas R;. Plant Cell. 2006;18:1681-1692. Paper describing PDB structure 2dt9. [2]. 19490113. Crystal structures of the regulatory subunit of Thr-sensitive aspartate kinase from Thermus thermophilus. Yoshida A, Tomita T, Kono H, Fushinobu S, Kuzuyama T, Nishiyama M;. FEBS J. 2009;276:3124-3136. Paper describing PDB structure 2dtj. [3]. 17350037. Structural Insight into concerted inhibition of alpha 2 beta 2-type aspartate kinase from Corynebacterium glutamicum. Yoshida A, Tomita T, Kurihara T, Fushinobu S, Kuzuyama T, Nishiyama M;. J Mol Biol. 2007;368:521-536. Paper describing PDB structure 2hmf. [4]. 17012784. The initial step in the archaeal aspartate biosynthetic pathway catalyzed by a monofunctional aspartokinase. Faehnle CR, Liu X, Pavlovsky A, Viola RE;. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006;62:962-966. Paper describing PDB structure 2j0w. [5]. 16905770. Structures of R- and T-state Escherichia coli aspartokinase III. Mechanisms of the allosteric transition and inhibition by lysine. Kotaka M, Ren J, Lockyer M, Hawkins AR, Stammers DK;. J Biol . TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

The ACT domain is a structural motif of 70-90 amino acids that functions in the control of metabolism, solute transport and signal transduction. They are thus found in a variety of different proteins in a variety of different arrangements [1]. In mammalian phenylalanine hydroxylase the domain forms no contacts but promotes an allosteric effect despite the apparent lack of ligand binding [2]. [1]. 16987805. The ACT domain: a small molecule binding domain and its role as a common regulatory element. Grant GA;. J Biol Chem. 2006;281:33825-33829. [2]. 18368466. Searching distant homologs of the regulatory ACT domain in phenylalanine hydroxylase. Siltberg-Liberles J, Martinez A;. Amino Acids. 2009;36:235-249. (from Pfam)

Date:

2024-10-16

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

aspartate kinase catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine

Date:

2017-07-10

Catalyzes the formation of 4-phospho-L-aspartate from L-aspartate and ATP; diaminopimelate sensitive

Gene:

dapG

Date:

2021-09-10

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

This model describes a subclass of aspartate kinases. These are mostly Lys-sensitive and not fused to homoserine dehydrogenase, unlike some Thr-sensitive and Met-sensitive forms. Homoserine dehydrogenase is part of Thr and Met but not Lys biosynthetic pathways. 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. The protein slr0657 from Synechocystis PCC6803 is extended by a duplication of the C-terminal region corresponding to the beta chain. Incorporation of a second copy of the C-terminal domain may be quite common in this subgroup of aspartokinases.

Date:

2021-04-27