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Enzyme Nomenclature
Information on EC 1.3.1.76 - precorrin-2 dehydrogenase
for references in articles please use BRENDA:EC1.3.1.76
Word Map on EC 1.3.1.76
- 1.3.1.76
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sirohaem
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uroporphyrinogen
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dehydrogenation
- cobalamin
- cobalt
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ferrochelation
- sirohydrochlorin
- tetrapyrrole
- sulfite
- megaterium
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prosthetic
- nitrite
- typhimurium
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reductases
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nad+-dependent
- cobaltochelatase
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.3.1.76
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RECOMMENDED NAME
GeneOntology No.
precorrin-2 dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
precorrin-2 + NAD+ = sirohydrochlorin + NADH + H+
first step; This enzyme catalyses the second of three steps leading to the formation of siroheme from uroporphyrinogen III. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and the third step involves the chelation of ferrous iron 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 SirC being responsible for the above reaction
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
precorrin-2:NAD+ oxidoreductase
This enzyme catalyses the second of three steps leading to the formation of siroheme from uroporphyrinogen III. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and the third step involves the chelation of ferrous iron 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 SirC being responsible for the above reaction.
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CAS REGISTRY NUMBER
COMMENTARY
227184-47-6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
formerly Rhizobium leguminosarum biovar phaseoli, wild-type strain CE3, mutant strain CTNUX8
SwissProt
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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
additional information
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large multifunctional protein that catalyzes four diverse reactions, 2 S-adensyl-L-methionine-dependent methylations, NAD+-dependent tetrapyrrole dehydrogenation and metal chelation
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
unlike Met8p and CysG, SirC has no chelatase actvity
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
siroheme and cobalamin biosynthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
unlike Met8p and CysG, SirC has no chelatase actvity
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
siroheme and cobalamin biosynthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
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multifunctional protein involved in S-adenosyl-L-methionine-dependent methylation, pyridine dinucleotide dependent dehydrogenation, and ferrochelation, second of three steps leading to formation of siroheme from uroporphyrinogen III
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
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multifunctional protein involved in S-adenosyl-L-methionine-dependent methylation, pyridine dinucleotide dependent dehydrogenation, and ferrochelation, second of three steps leading to formation of siroheme from uroporphyrinogen III
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
second of three steps leading to formation of siroheme from uroporphyrinogen III
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
bifunctional dehydrogenase and ferrochelatase, second of three steps leading to formation of siroheme from uroporphyrinogen III
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
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siroheme and cobalamin biosynthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
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tetrapyrrole and cobalamin biosynthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
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precorrin-2 is the precursor of both siroheme and B12, first reaction specific to B12 synthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
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?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
P61818
siroheme and cobalamin biosynthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
P61818
siroheme and cobalamin biosynthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
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multifunctional protein involved in S-adenosyl-L-methionine-dependent methylation, pyridine dinucleotide dependent dehydrogenation, and ferrochelation, second of three steps leading to formation of siroheme from uroporphyrinogen III
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
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multifunctional protein involved in S-adenosyl-L-methionine-dependent methylation, pyridine dinucleotide dependent dehydrogenation, and ferrochelation, second of three steps leading to formation of siroheme from uroporphyrinogen III
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
O50477
second of three steps leading to formation of siroheme from uroporphyrinogen III
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
P15807
bifunctional dehydrogenase and ferrochelatase, second of three steps leading to formation of siroheme from uroporphyrinogen III
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
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siroheme and cobalamin biosynthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
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tetrapyrrole and cobalamin biosynthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
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?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
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precorrin-2 is the precursor of both siroheme and B12, first reaction specific to B12 synthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
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enzyme catalyzes cobalt insertion leading to B12 synthesis
Fe2+
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enzyme catalyzes iron insertion leading to siroheme synthesis
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
orthorhombic space group P2(1)2(1)2(1), unit cell dimensions a = 60.73 A, b = 121.49 A, c = 130.79 A
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
MET8 mutants complemented by Salmonella typhimurium cysG, cloned and expressed in Escherichia coli
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sequenced and overproduced, sirABC gene cluster complements Escherichia coli cysG mutants
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.1.76)
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