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

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
2.1.1.196
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RECOMMENDED NAME
GeneOntology No.
cobalt-precorrin-6B (C15)-methyltransferase [decarboxylating]
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cobalt-precorrin-6B + S-adenosyl-L-methionine = cobalt-precorrin-7 + S-adenosyl-L-homocysteine + CO2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
cob(II)yrinate a,c-diamide biosynthesis I (early cobalt insertion)
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vitamin B12 metabolism
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Porphyrin and chlorophyll metabolism
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:precorrin-6B C15-methyltransferase (C-12-decarboxylating)
This enzyme catalyses both methylation at C-15 and decarboxylation of the C-12 acetate side chain of cobalt-precorrin-6B, a step in the anaerobic (early cobalt insertion) adenosylcobalamin biosynthesis pathway.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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the enzyme plays two roles, as a cobalt-precorrin-7 C15-methyltransferase and a C12-decarboxylase to produce the intermediate cobalt-precorrin-8
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cobalt-precorrin-6B + S-adenosyl-L-methionine
cobalt-precorrin-7 + S-adenosyl-L-homocysteine + CO2
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cobalt-precorrin-6B + S-adenosyl-L-methionine
cobalt-precorrin-7 + S-adenosyl-L-homocysteine + CO2
show the reaction diagram
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?
PDB
SCOP
CATH
ORGANISM
UNIPROT
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
Show AA Sequence (212 entries)
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