Information on EC 2.1.1.271 - cobalt-precorrin-4 methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.271
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RECOMMENDED NAME
GeneOntology No.
cobalt-precorrin-4 methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cobalt-precorrin-4 = S-adenosyl-L-homocysteine + cobalt-precorrin-5A
show the reaction diagram
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S-adenosyl-L-methionine + precorrin-4 = S-adenosyl-L-homocysteine + precorrin-5
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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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:cobalt-precorrin-4 11-methyltransferase
Part of the anaerobic route to adenosylcobalamin.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene cbiF
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Manually annotated by BRENDA team
i.e. Propionibacterium shermanii, gene cbiF
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Manually annotated by BRENDA team
gene cobM
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
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His-tagged protein is able to complement a Salmonella typhimurium cbiF mutant
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + cobalt-precorrin-4
S-adenosyl-L-homocysteine + cobalt-precorrin-5
show the reaction diagram
S-adenosyl-L-methionine + cobalt-precorrin-4
S-adenosyl-L-homocysteine + cobalt-precorrin-5A
show the reaction diagram
S-adenosyl-L-methionine + precorrin-4
S-adenosyl-L-homocysteine + precorrin-5
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
S-adenosyl-L-methionine + cobalt-precorrin-4
S-adenosyl-L-homocysteine + cobalt-precorrin-5
show the reaction diagram
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enzyme is involved in anaerobic cobalamin, i.e. vitamin B12, biosynthesis, pathway overview
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?
S-adenosyl-L-methionine + cobalt-precorrin-4
S-adenosyl-L-homocysteine + cobalt-precorrin-5A
show the reaction diagram
S-adenosyl-L-methionine + precorrin-4
S-adenosyl-L-homocysteine + precorrin-5
show the reaction diagram
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enzyme is involved in aerobic cobalamin, i.e. vitamin B12, biosynthesis, pathway overview
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62000
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gel filtration; gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 31000, SDS-PAGE; 2 * 31000, SDS-PAGE, recombinant protein including His-tag
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; to 2.4 A resolution. Protein shows two discrete crystal forms, and crystals only grow in the presence of either S-adenosyl-L-methionine or S-adenosyl-L-homocysteine
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; to 2.4 A resolution. The enzyme contains two alpha/beta domains forming a trough in which S-adenosyl-L-homocysteine binds. The entire structure follows a beta-alpha repeating pattern with the single exception of a beta-hairpin late in the C-terminal domain. A second crystal form determined at 3.1 A resolution highlights the flexibility of two loops around the S-adenosyl-L-homocysteine-binding site
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to freezing at -20°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, protein reduced in volume to a concentration in excess of 10 mg/ml is stable to freezing and remains in solution when thawed
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4°C, protein can be stored for several weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli; overexpression in Escherichia coli
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gene cbiF, 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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information