HOME
login
history
all enzymes
BRENDA home
History
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
-
sirohaem
- cobalamin
-
dehydrogenation
- cobalt
-
uroporphyrinogen
-
ferrochelation
- sirohydrochlorin
- tetrapyrrole
-
prosthetic
- megaterium
- nitrite
- sulfite
-
nad+-dependent
- cobaltochelatase
-
reductases
- typhimurium
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.3.1.76
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
precorrin-2 dehydrogenase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
227184-47-6
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
formerly Rhizobium leguminosarum biovar phaseoli, wild-type strain CE3, mutant strain CTNUX8
SwissProt
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
?
-
-
large multifunctional protein that catalyzes four diverse reactions, 2 S-adensyl-L-methionine-dependent methylations, NAD+-dependent tetrapyrrole dehydrogenation and metal chelation
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
unlike Met8p and CysG, SirC has no chelatase actvity
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
siroheme and cobalamin biosynthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
unlike Met8p and CysG, SirC has no chelatase actvity
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
siroheme and cobalamin biosynthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
-
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
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
-
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
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
second of three steps leading to formation of siroheme from uroporphyrinogen III
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
bifunctional dehydrogenase and ferrochelatase, second of three steps leading to formation of siroheme from uroporphyrinogen III
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
-
siroheme and cobalamin biosynthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
-
tetrapyrrole and cobalamin biosynthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
-
-
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
-
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
P61818
siroheme and cobalamin biosynthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
-
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
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
-
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
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
O50477
second of three steps leading to formation of siroheme from uroporphyrinogen III
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
P15807
bifunctional dehydrogenase and ferrochelatase, second of three steps leading to formation of siroheme from uroporphyrinogen III
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
-
siroheme and cobalamin biosynthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
-
tetrapyrrole and cobalamin biosynthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
-
?
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
-
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
enzyme catalyzes cobalt insertion leading to B12 synthesis
Fe2+
-
enzyme catalyzes iron insertion leading to siroheme synthesis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
ORGANISM
UNIPROT
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
MET8 mutants complemented by Salmonella typhimurium cysG, cloned and expressed in Escherichia coli
-
sequenced and overproduced, sirABC gene cluster complements Escherichia coli cysG mutants
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 1.3.1.76)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
