2.1.1.196: cobalt-precorrin-6B (C15)-methyltransferase [decarboxylating]

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For detailed information about cobalt-precorrin-6B (C15)-methyltransferase [decarboxylating], go to the full flat file.

Reaction

Synonyms

CbiE, CbiT

ECTree

     2 Transferases

         2.1 Transferring one-carbon groups

             2.1.1 Methyltransferases

                2.1.1.196 cobalt-precorrin-6B (C15)-methyltransferase [decarboxylating]

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667	AA Sequence
2	Application
1	Crystallization (Commentary)
1	General Information
1	Natural Substrates/ Products (Substrates)
4	Organism
5	Pathway
1	Reaction
4	Reference
1	Substrates and Products (Substrate)
3	Synonyms
1	Systematic Name

Crystallization

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Crystallization on EC 2.1.1.196 - cobalt-precorrin-6B (C15)-methyltransferase [decarboxylating]

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

homotetrameric apo form of CbiT crystallized in several space groups, to about 2.5 A resolution, and in complex with S-adenosyl-L-homocysteine, to 1.9 A resolution. The protein shows structural similarity to Rossmann-like S-adenosyl-methionine-dependent methyltransferases, and the cocrystal structure shows that it binds S-adenosyl-methionine in standard geometry near a binding pocket that can accommodate a precorrin substrate. CbiT probably functions as a precorrin methyltransferase

Methanothermobacter thermautotrophicus

O26249

660514