2.1.1.107: uroporphyrinogen-III C-methyltransferase
This is an abbreviated version!
For detailed information about uroporphyrinogen-III C-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.107
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2.1.1.107
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precorrin-2
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siroheme
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denitrificans
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cobalamin
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nitrite
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sirohydrochlorin
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tetrapyrrole
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chelatase
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ferrochelatase
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corrin
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transmethylation
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corrinoid
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dissimilatory
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ferrochelation
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analysis
- 2.1.1.107
- precorrin-2
- siroheme
- denitrificans
- cobalamin
- nitrite
- sirohydrochlorin
- tetrapyrrole
- chelatase
-
ferrochelatase
-
corrin
-
transmethylation
- corrinoid
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dissimilatory
-
ferrochelation
- analysis
Reaction
2 S-adenosyl-L-methionine
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Synonyms
adenosylmethionine-uroporphyrinogen III methyltransferase, At5g40850, CobA, CobA/HemD, CysG, HemD-CobA, NirE, S-adenosyl-L-methionine dependent uroporphyrinogen III methylase, S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferase, S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase, S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase, SAM-dependent uroporphyrinogen III methyltransferase, sirohaem synthase, SUMT, UMT, UPM1, UroM, uroporphyrinogen III C-methyltransferase, uroporphyrinogen III methylase, uroporphyrinogen III methyltransferase, uroporphyrinogen III methyltransferase/synthase, uroporphyrinogen III synthase/methyltransferase, uroporphyrinogen methyltransferase,
ECTree
2.1.1.107 uroporphyrinogen-III C-methyltransferaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.1.1.107 - uroporphyrinogen-III C-methyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G12A
E114Q
G189K
G189N
H161F
the mutant shows reduced activity compared to the wild type enzyme
K102A
the mutant shows no activity and strongly reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme
M186L
R111K
R149K
the mutant shows no activity compared to the wild type enzyme
R51D
residue R51 is mainly involved in stabilization of the propionate side chain of ring A by hydrophobic interactions with an average distance of 4.1 A. In the mutant R51K, the side chain of K51 makes stable electrostatic interactions with the acetate side chain of ring A, however there are no hydrophobic interactions
R51K
the mutant shows reduced activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme
D47N
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binds about a quarter the quantity of S-adenosyl-L-methionine compared with wild-type, reaction product is only poxidised precorrin-1
F106A
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considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzymic activity
L49A
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binds about half the quantity of S-adenosyl-L-methionine compared with wild-type, reaction products are oxidised forms of both precorrin-1 and precorrin-2
T130A
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considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine
Y183A
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considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzyminc activity
additional information
G12A
site-directed mutagenesis of cobA abolishes the tellurite resistance of the mesophilic, heterologous host Escherichia coli and the SUMT activity in vitro. Cells overexpressing SUMT G12A show 7fold less tolerance to K2TeO3 as compared to that exhibit by cells expressing the wild-type methyltransferase
G12A
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site-directed mutagenesis of cobA abolishes the tellurite resistance of the mesophilic, heterologous host Escherichia coli and the SUMT activity in vitro. Cells overexpressing SUMT G12A show 7fold less tolerance to K2TeO3 as compared to that exhibit by cells expressing the wild-type methyltransferase
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E114Q
the mutant shows strongly reduced activity compared to the wild type enzyme
E114Q
increase in the root mean square deviations of the uroporphyrinogen III substrate in respect to the wild-type
G189K
the mutant shows increased activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme
G189K
increase in activity compared to wild-type. The side chain of K189 makes electrostatic interactions with the propionate side chain of ring B with an average distance of 4.0 A. The backbone of K189 makes hydrogen bonds with the propionate side chain of ring B of uroporphyrinogen III
G189N
the mutant shows increased activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme
G189N
increase in activity compared to wild-type. Both side chain and the backbone of N189 residue participates in hydrogen bonds with the propionate side chain of ring B of uroporphyrinogen III
M186L
the mutant shows strongly reduced activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme
M186L
loss of hydrophobic interactions between the side chain of L186 and methyl group of SAM
R111K
the mutant shows strongly reduced activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme
R111K
the side chain of residue R111 stabilizes the uroporphyrinogen III ring A acetate side chain by electrostatic interactions. Mutant R111K makes very unstable interactions with an average distance of 5 A between the acetate of ring A of uroporphyrinogen III
additional information
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separation of the individual enzyme activities, uroporphyrinogen III synthase and uroporphyrinogen III methyltransferase, by dissecting the relevant gene to allow the production of two distinct proteins
additional information
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construction of a nirE transposon mutant, which is not complemented by native cobA encoding the SAM-dependent uroporphyrinogen III methyltransferase involved in cobalamin formation, overview
additional information
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deletion mutants, truncated one deleting the C-terminal extra 52 amino acids actively expressed in Escherichia coli, the mature SUMT fusion mutant or the mature SUMT deleting the N-terminal 36 amino acids including glycine-rich region involved directly in SAM binding expressed as an inclusion body in Escherichia coli
