Information on EC 2.1.1.132 - precorrin-6B C5,15-methyltransferase (decarboxylating)

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

EC NUMBER
COMMENTARY hide
2.1.1.132
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RECOMMENDED NAME
GeneOntology No.
precorrin-6B C5,15-methyltransferase (decarboxylating)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + precorrin-6B = 2 S-adenosyl-L-homocysteine + precorrin-8X + CO2
show the reaction diagram
S-adenosyl-L-methionine + precorrin-6B = S-adenosyl-L-homocysteine + precorrin-7 + CO2
show the reaction diagram
(1a)
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S-adenosyl-L-methionine + precorrin-7 = S-adenosyl-L-homocysteine + precorrin-8X
show the reaction diagram
(1b)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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Porphyrin and chlorophyll metabolism
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vitamin B12 metabolism
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:1-precorrin-6B C5,15-methyltransferase (C-12-decarboxylating)
The enzyme, which participates in the aerobic adenosylcobalamin biosynthesis pathway, has S-adenosyl-L-methionine-dependent methyltransferase and decarboxylase activities. The enzyme is a fusion protein with two active sites; one catalyses the methylation at C15 and the decarboxylation, while the other catalyses the methylation at C5.
CAS REGISTRY NUMBER
COMMENTARY hide
150474-63-8
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150474-63-8
protein (Salmonella typhimurium clone pJO gene cbiE reduced) /GenBank L12005-derived protein /methyltransferase precorrin 6y (Salmonella typhimurium strain LT2 gene cbiE)
150474-64-9
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150474-64-9
genbank L12006-derived protein /protein (Salmonella typhimurium clone pJO26 gene cbiT reduced) /methyltransferase, precorrin 6y (Salmonella typhimurium strain LT2 gene cbiT)
162995-22-4
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181889-87-2
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181889-87-2
methyltransferase, precorrin 6y (Methanococcus jannaschii) /genBank U67594-derived protein GI 1500413
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene MT0146 or cbiT, fused to gene cbiE, resulting in cobL
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Manually annotated by BRENDA team
i.e. Propionibacterium shermanii, gene cbiE
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Manually annotated by BRENDA team
strain SC510 Rifr harboring plasmid pXL253
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Adenosyl-L-methionine + precorrin-6Y
?
show the reaction diagram
Adenosyl-L-methionine + precorrin-6Y
Adenosyl-L-homocysteine + precorrin-8X + CO2
show the reaction diagram
S-adenosyl-L-methionine + cobalt-precorrin-6Y + 6 H+
S-adenosyl-L-homocysteine + cobalt-precorrin-8X + 2 H2O
show the reaction diagram
additional information
?
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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
Adenosyl-L-methionine + precorrin-6Y
?
show the reaction diagram
S-adenosyl-L-methionine + cobalt-precorrin-6Y + 6 H+
S-adenosyl-L-homocysteine + cobalt-precorrin-8X + 2 H2O
show the reaction diagram
additional information
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0022
Precorrin-6Y
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210)
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21000
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4 * 21000, static light scattering and SDS-PAGE
42900
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x * 42900, calculation from nucleotide sequence
42952
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2 * 42952, calculation from nucleotide sequence
43000
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x * 43000, SDS-PAGE
81000
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static light scattering
320000
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HPLC gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 42952, calculation from nucleotide sequence
tetramer
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4 * 21000, static light scattering and SDS-PAGE
additional information
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CbiT has a Rossmann-like methyltransferase fold, possessing a tetramerization domain, structure overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant apo-enzyme CbiT or in complex with S-adenosyl-L-methionine, hanging drop vapour diffusion method, 25°C, for the apo-enzyme: 5-10 mg/ml protein in 10% w/v PEG 8000, 100 mM MgCl2, and 5 mM Tric-HCl, pH 7.5, 0.002 ml equilibrated against 1 ml of well solution containing 16-22% PEG 8000, 0.2 M MgCl2, 10 mM Tris-HCl, pH 7.5, crystals appear after 1 day, for the binary complex: 1-2 mg/ml protein in 0.5 mM S-adenosyl-L-methionine, 0.1-0.2% PEG 8000, 50 mM MgCl2, 2.5 mM Tris-HCl, pH 7.5, 0.004 ml equilibrated against 1 ml of well solution containing 0.2-0.4% PEG 8000, 0.2 M MgCl2, and 5 mM Tris-HCl, pH 7.5, cryoprotection by soaking in 25% PEG 8000, 0.2 M MgCl2, and glycerol up to 25% w/v, freezing in liquid propane, X-ray diffraction structure determination and analysis at 1.9 A resolution, modeling
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme CbiT from Escherichia coli strain B834
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene MT0146 or cbiT, fused to gene cbiE, resulting in cobL, DNA and amino acid sequence determination and analysis, promotor analysis, expression in Escherichia coli strain B834
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genes cbiEGH and cbiT, the gene cbiE of Propionibacterium freudenreichii is organized in a single ORF with genes cbiH and cbiG, DNA and amino acid sequence determination and analysis, genetic organization, co-overexpression of enzymes and reconstruction of the anaerobic cobalamin biosynthetic pathway in Escherichia coli in a construct comprising several genes, overview
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overexpression in Escherichia coli
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