Protein Family Models

This is the N-terminal regulatory domain of bacterial isocitrate dehydrogenase kinase/phosphatase (AceK) proteins (EC:2.7.1.116) [1,2]. It has an alpha-helical fold, with two long, parallel alpha-helices that form a large hairpin structure followed by two short, parallel alpha-helices forming a small hairpin segment. This domain is linked to the C-terminal kinase domain by a short (27 residues) alpha-helix [2]. [1]. 9409817. Size and sequence polymorphism in the isocitrate dehydrogenase kinase/phosphatase gene (aceK) and flanking regions in Salmonella enterica and Escherichia coli. Nelson K, Wang FS, Boyd EF, Selander RK;. Genetics 1997;147:1509-1520. [2]. 20505668. Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase. Zheng J, Jia Z;. Nature. 2010;465:961-965. (from Pfam)

Date:

2024-10-16

This the C-terminal protein kinase domain of bacterial isocitrate dehydrogenase kinase/phosphatase (AceK) proteins (EC:2.7.1.116) [1,2]. It has a classic bi-lobe protein kinase fold with the ATP-binding cleft located at the interface between the two lobes. The N-terminal lobe comprises a twisted antiparallel beta-sheet of five strands and two alpha-helices. The C-terminal lobe is larger and mainly alpha-helical, with some stretches of antiparallel beta-strands [2]. [1]. 9409817. Size and sequence polymorphism in the isocitrate dehydrogenase kinase/phosphatase gene (aceK) and flanking regions in Salmonella enterica and Escherichia coli. Nelson K, Wang FS, Boyd EF, Selander RK;. Genetics 1997;147:1509-1520. [2]. 20505668. Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase. Zheng J, Jia Z;. Nature. 2010;465:961-965. (from Pfam)

Date:

2024-10-16

bifunctional isocitrate dehydrogenase kinase/phosphatase catalyzes the phophoryation/dephosphorylation of isocitrate dehydrogenase

Date:

2016-10-31

Catalyzes the phosphorylation/dephosphorylation of the enzyme isocitrate dehydrogenase on a specific serine which regulates activity

Gene:

aceK

Date:

2021-07-29