Literature summary extracted from

Liebold, C.; List, F.; Kalbitzer, H.R.; Sterner, R.; Brunner, E.
The interaction of ammonia and xenon with the imidazole glycerol phosphate synthase from Thermotoga maritima as detected by NMR spectroscopy (2010), Protein Sci., 19, 1774-1782 .

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
4.3.2.10	expression in Escherichia coli BL21(DE3)	Thermotoga maritima

Protein Variants

EC Number	Protein Variants	Comment	Organism
4.3.2.10	T78M	mutant enzyme with reduced catalytic activity	Thermotoga maritima

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.3.2.10	Thermotoga maritima	Q9X0C6 AND Q9X0C8	Q9X0C6: subunit HisF, Q9X0C8: subunit HisH	-
4.3.2.10	Thermotoga maritima ATCC 43589	Q9X0C6 AND Q9X0C8	Q9X0C6: subunit HisF, Q9X0C8: subunit HisH	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
4.3.2.10	-	Thermotoga maritima

Subunits

EC Number	Subunits	Comment	Organism
4.3.2.10	dimer	the enzyme is a 1:1 complex of the glutaminase subunit HisH and the cyclase subunit HisF. Subunit HisF contains three distinct internal cavities, which can be identified by xenon-induced chemical shift changes of the neighboring amino acid residues. Two of these cavities are located at the active site at opposite ends of the substrate N'-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide binding groove. The third cavity is located in the interior of the central beta-barrel of HisF and overlaps with the putative ammonia transport channel	Thermotoga maritima

Synonyms

EC Number	Synonyms	Comment	Organism
4.3.2.10	ImGP synthase	-	Thermotoga maritima

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Release 2023.1 (January 2023)