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Information on EC 2.1.1.107 - uroporphyrinogen-III C-methyltransferase
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2.1.1.107 uroporphyrinogen-III C-methyltransferaseIUBMB Comments
This enzyme catalyses two sequential methylation reactions, the first forming precorrin-1 and the second leading to the formation of precorrin-2. It is the first of three steps leading to the formation of siroheme from uroporphyrinogen III. The second step involves an NAD+-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76, precorrin-2 dehydrogenase) and the third step involves the chelation of Fe2+ to sirohydrochlorin to form siroheme (EC 4.99.1.4, sirohydrochlorin ferrochelatase). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalysed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirA being responsible for the above reaction. Also involved in the biosynthesis of cobalamin.
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Word Map
- 2.1.1.107
- precorrin-2
- siroheme
- denitrificans
- cobalamin
- nitrite
- sirohydrochlorin
- tetrapyrrole
- chelatase
-
ferrochelatase
-
corrin
-
transmethylation
- corrinoid
-
dissimilatory
-
ferrochelation
- analysis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
uroporphyrinogen iii methyltransferase, s-adenosyl-l-methionine:uroporphyrinogen iii methyltransferase, uroporphyrinogen iii methylase, uroporphyrinogen-iii c-methyltransferase, s-adenosyl-l-methionine uroporphyrinogen iii methyltransferase, sam-dependent uroporphyrinogen iii methyltransferase, sirohaem synthase, uroporphyrinogen iii synthase/methyltransferase, uroporphyrinogen iii c-methyltransferase, s-adenosyl-l-methionine-dependent uroporphyrinogen iii methyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosylmethionine-uroporphyrinogen III methyltransferase
-
-
-
-
CobA/HemD
CysG
NirE
S-adenosyl-L-methionine dependent uroporphyrinogen III methylase
-
-
-
-
S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferase
-
S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase
-
sirohaem synthase
-
-
-
-
SUMT
UMT
UroM
uroporphyrinogen III C-methyltransferase
-
-
-
-
uroporphyrinogen III methylase
-
-
-
-
uroporphyrinogen III methyltransferase
uroporphyrinogen III synthase/methyltransferase
uroporphyrinogen methyltransferase,
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + uroporphyrinogen III = 2 S-adenosyl-L-homocysteine + precorrin-2
overall reaction
-
-
-
S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2
(1b)
-
-
-
S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1
(1a)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:uroporphyrinogen-III C-methyltransferase
This enzyme catalyses two sequential methylation reactions, the first forming precorrin-1 and the second leading to the formation of precorrin-2. It is the first of three steps leading to the formation of siroheme from uroporphyrinogen III. The second step involves an NAD+-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76, precorrin-2 dehydrogenase) and the third step involves the chelation of Fe2+ to sirohydrochlorin to form siroheme (EC 4.99.1.4, sirohydrochlorin ferrochelatase). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalysed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirA being responsible for the above reaction. Also involved in the biosynthesis of cobalamin.
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CAS REGISTRY NUMBER
COMMENTARY
73665-99-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
S-adenosyl-L-methionine + heptacarboxyporphyrinogen III
?
-
-
-
-
?
S-adenosyl-L-methionine + hexacarboxyporphyrinogen III
?
-
-
-
-
?
S-adenosyl-L-methionine + pentacarboxyporphyrinogen III
?
-
-
-
-
?
S-adenosyl-L-methionine + precorrin-1
S-adenosyl-L-homocysteine + precorrin-2
-
-
-
?
S-adenosyl-L-methionine + precorrin-2
S-adenosyl-L-homocysteine + trimethylpyrrocorphin
-
-
-
-
?
S-adenosyl-L-methionine + uroporphyrinogen III
S-adenosyl-L-homocysteine + precorrin-1
-
-
-
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
Q96532
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
Q96532
involved in biosynthesis of siroheme
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
Q96532
no synthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
methylates positions 2 and 7
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
methylates positions 2 and 7
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
methylates positions 2 and 7
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
methylates positions 2 and 7
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of sirohydrochlorin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of sirohydrochlorin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
after prolonged incubation (15 h) also tri- and tetra-methylated compounds formed, third methyl group at position 12, product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
involved in biosynthesis of sirohydrochlorin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
produces equal amounts of precorrin-1 and precorrin-2, product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of siroheme
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of siroheme
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
-
-
-
-
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
overall reaction
-
-
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
-
-
-
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
-
-
-
ir
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
-
-
-
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
-
-
-
?
S-adenosyl-L-methionine + uroporphyrinogen I
?
-
methylates positions 2 and 7
-
-
?
S-adenosyl-L-methionine + uroporphyrinogen I
?
methylates positions 2 and 7
-
-
?
S-adenosyl-L-methionine + uroporphyrinogen I
?
-
-
-
-
?
uroporphyrinogen III + S-adenosyl-L-methionine
precorrin-2 + S-adenosyl-L-homocysteine
-
via precorrin-1
-
-
?
uroporphyrinogen III + S-adenosyl-L-methionine
precorrin-2 + S-adenosyl-L-homocysteine
the enzyme binds S-adenosyl-L-methionine and catalyzes the production of III methyl uroporphyrinogen in vitro
-
-
?
uroporphyrinogen III + S-adenosyl-L-methionine
precorrin-2 + S-adenosyl-L-homocysteine
the enzyme binds S-adenosyl-L-methionine and catalyzes the production of III methyl uroporphyrinogen in vitro
-
-
?
uroporphyrinogen III + S-adenosyl-L-methionine
precorrin-2 + S-adenosyl-L-homocysteine
-
-
-
-
?
uroporphyrinogen III + S-adenosyl-L-methionine
precorrin-2 + S-adenosyl-L-homocysteine
-
NirE binds S-adenosyl-L-methionine, although not with the same avidity as reported for other SAM-dependent uroporphyrinogen III methyltransferases involved in siroheme and cobalamin biosynthesis
-
-
?
additional information
?
-
Q96532
no formation of sirohydrochlorin in presence of NAD+ or NADP+
-
-
?
additional information
?
-
-
no formation of sirohydrochlorin in presence of NAD+ or NADP+
-
-
?
additional information
?
-
-
uroporphyrinogen III synthase is fused to uroporphyrinogen III methyltransferase in Desulfovibrio vulgaris
-
-
?
additional information
?
-
-
at high enzyme concentrations NirE catalyzes an overmethylation of uroporphyrinogen III, resulting in the formation of trimethylpyrrocorphin
-
-
?
additional information
?
-
-
uroporphyrin III is not a substrate of the enzyme
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
S-adenosyl-L-methionine + precorrin-1
S-adenosyl-L-homocysteine + precorrin-2
-
-
-
?
S-adenosyl-L-methionine + precorrin-2
S-adenosyl-L-homocysteine + trimethylpyrrocorphin
-
-
-
-
?
S-adenosyl-L-methionine + uroporphyrinogen III
S-adenosyl-L-homocysteine + precorrin-1
-
-
-
?
additional information
?
-
-
uroporphyrinogen III synthase is fused to uroporphyrinogen III methyltransferase in Desulfovibrio vulgaris
-
-
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
Q96532
involved in biosynthesis of siroheme
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
Q96532
no synthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of sirohydrochlorin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of sirohydrochlorin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
involved in biosynthesis of sirohydrochlorin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of siroheme
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of siroheme
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
-
-
-
-
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
overall reaction
-
-
?
uroporphyrinogen III + S-adenosyl-L-methionine
precorrin-2 + S-adenosyl-L-homocysteine
-
via precorrin-1
-
-
?
uroporphyrinogen III + S-adenosyl-L-methionine
precorrin-2 + S-adenosyl-L-homocysteine
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
complete inhibition by 0.1 mM, mechanism unclear
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-homocysteine
-
product inhibition at concentrations above 0.002 mM
uroporphyrinogen III
-
substrate inhibition at concentrations above 0.017 mM
uroporphyrinogen III
-
substrate inhibition above 0.002 mM
additional information
no substrate inhibition at uroporphyrinogen III concentrations of up to 0.02 mM
-
additional information
-
no substrate inhibition at uroporphyrinogen III concentrations of up to 0.02 mM
-
additional information
-
no inhibition by cobalamine or intermediates of synthesis
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00124
uroporphyrinogen III
pH 8.0, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
the enzyme is important in the heme d1 biosynthesis, the essential prosthetic group of the dissimilatory nitrite reductase cytochrome cd1 requiring the methylation of the tetrapyrrole precursor uroporphyrinogen III at positions C-2 and C-7, pathway overview
metabolism
-
the enzyme is involved in the tetrapyrrole biosynthesis. Uroporphyrinogen III represents the first branch point in the pathway, where the action of enzymes such as HemE, F (N) and G results in the formation of protoporphyrin IX, a precursor of modified tetrapyrroles such as haem and chlorophyll. Alternatively, uroporphyrinogen III can undergo a S-adenosylmethionine-dependent transmethylation positions 2 and 7, by CysG, Met1p or CobA depending on the organism, to generate precorrin-2, a highly unstable yellow dipyrrocorphin, overview
metabolism
-
uroporphyrinogen III synthase/methyltransferase is a key bifunctional enzyme in the biosynthesis of cobalamin and other tetrapyrrols
metabolism
Limosilactobacillus reuteri CRL 1098
-
uroporphyrinogen III synthase/methyltransferase is a key bifunctional enzyme in the biosynthesis of cobalamin and other tetrapyrrols
-
physiological function
the role of SUMT methyltransferase in tellurite(ate) detoxification is not related to tellurium volatilization
physiological function
-
enzyme overexpression confers resistance of the Escherichia coli cells to potassium tellurite that inhibits cell growth
physiological function
-
overexpression of UPM1 signals higher nitrite reductase (NII) and sulfite reductase gene and gene product expression. Increased NII expression regulates and enhances the transcript and protein abundance of nitrate reductase. Due to higher N and S assimilation in these plants, total protein content increases. Consequently, chlorophyll biosynthesis increases and upregulates photosynthetic electron transport and carbon assimilation. In the antisense plants, the transcript abundance, and protein content of nitrite reductase (NII) and sulfite reductase decrease, resulting in reduced total protein and chlorophyll content
physiological function
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the role of SUMT methyltransferase in tellurite(ate) detoxification is not related to tellurium volatilization
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