Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
glycine cleavage T C-terminal barrel domain-containing protein
This is a family of glycine cleavage T-proteins, part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes. GCV catalyses the catabolism of glycine in eukaryotes. The T-protein is an aminomethyl transferase. [1]. 9047339. Cloning, and molecular characterization of the GCV1 gene encoding the glycine cleavage T-protein from Saccharomyces cerevisiae. McNeil JB, Zhang F, Taylor BV, Sinclair DA, Pearlman RE, Bognar AL;. Gene 1997;186:13-20. (from Pfam)
Aminomethyltransferase folate-binding domain
glycine cleavage system aminomethyltransferase GcvT
glycine cleavage system aminomethyltransferase GcvT is a component of glycine cleavage system that catalyzes the degradation of glycine
Catalyzes the transfer of a methylene carbon from the methylamine-loaded GcvH protein to tetrahydrofolate, causing the release of ammonia and the generation of reduced GcvH protein
The glycine cleavage system T protein (GcvT) is also known as aminomethyltransferase (EC 2.1.2.10). It works with the H protein (GcvH), the P protein (GcvP), and lipoamide dehydrogenase. The reported sequence of the member from Aquifex aeolicus starts about 50 residues downstream of the start of other members of the family (perhaps in error); it scores below the trusted cutoff. Eukaryotic forms are mitochondrial and have an N-terminal transit peptide.
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on