Literature summary for 1.4.1.27 extracted from

Lee, H.H.; Kim, D.J.; Ahn, H.J.; Ha, J.Y.; Suh, S.W.
Crystal structure of T-protein of the glycine cleavage system. Cofactor binding, insights into H-protein recognition, and molecular basis for understanding nonketotic hyperglycinemia (2004), J. Biol. Chem., 279, 50514-50523 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of component T-protein in the apoform, the tetrahydrofolate complex, the folinic acid complex, and the lipoic acid complex. Tetrahydrofolate (or folinic acid) is bound near the center of the tripartite T-protein. Lipoic acid is bound adjacent to the tetrahydrofolate binding pocket, thus defining the interaction surface for H-protein binding	Thermotoga maritima

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Thermotoga maritima	Q9WY54	i.e. aminomethyltransferase component T-protein, cf. EC 2.1.2.10	-

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Release 2023.1 (January 2023)