Information on EC 2.1.1.272 - cobalt-factor III methyltransferase

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The expected taxonomic range for this enzyme is: Bacillus megaterium

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EC NUMBER
COMMENTARY hide
2.1.1.272
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RECOMMENDED NAME
GeneOntology No.
cobalt-factor III methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cobalt-factor III + reduced acceptor = S-adenosyl-L-homocysteine + cobalt-precorrin-4 + acceptor
show the reaction diagram
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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:cobalt-factor III 17-methyltransferase (ring contracting)
Isolated from Bacillus megaterium. The enzyme catalyses both methylation at C-17 and ring contraction. Contains a [4Fe-4S] cluster. It can also convert cobalt-precorrin-3 to cobalt-precorrin-4. The reductant may be thioredoxin.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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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(II)-factor-III + dithiothreitol
S-adenosyl-L-homocysteine + cobalt(II)-precorrin-4 + oxidized dithiothreitol
show the reaction diagram
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?
S-adenosyl-L-methionine + cobalt(II)-precorrin-3
S-adenosyl-L-homocysteine + cobalt(II)-factor-IV
show the reaction diagram
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?
additional information
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top print hide
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
[4Fe-4S]-center
enzyme contains a [4Fe-4S]-center required for ring contraction reaction. Iron content is 4.8 mol of iron/mol of enzyme
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
x * 65000, SDS-PAGE of recombinant enzyme including His-tag
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 65000, SDS-PAGE of recombinant enzyme including His-tag
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Bacillus megaterium DSM319
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C402A
mutation introduced to disrupt the iron-sulfur center. Mutant lacks any visible coloration and has decreased absorbance between 350 and 420 nm and less than 95% of wild-type activity
C443A
mutation introduced to disrupt the iron-sulfur center. Mutant lacks any visible coloration and has decreased absorbance between 350 and 420 nm and less than 95% of wild-type activity
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LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.272)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)