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Information on EC 1.3.1.76 - precorrin-2 dehydrogenase and Organism(s) Priestia megaterium and UniProt Accession P61818

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IUBMB Comments
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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Priestia megaterium
UNIPROT: P61818
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The taxonomic range for the selected organisms is: Priestia megaterium
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
met8p, siroheme synthase, precorrin-2 dehydrogenase, cysg enzyme, cysg gene product, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
precorrin-2 dehydrogenase
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CysG
-
-
-
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Met8p
-
-
-
-
SirC
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
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reduction
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
227184-47-6
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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
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
precorrin-2 + NAD+
sirohydrochlorin + NADH + H+
show the reaction diagram
siroheme and cobalamin biosynthesis, second of three steps leading to formation of siroheme from uroporphyrinogen III
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SIRC_PRIMG
202
0
22970
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
2 * 22000, homodimer, SDS-PAGE
45000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 22000, homodimer, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+ chelating column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)pLysS(codon+) cells
sequenced and overproduced, sirABC gene cluster complements Escherichia coli cysG mutants
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Raux, E.; Leech, H.K.; Beck, R.; Schubert, H.L.; Santander, P.J.; Roessner, C.A.; Scott, A.I.; Martens, J.H.; Jahn, D.; Thermes, C.; Rambach, A.; Warren, M.J.
Identification and functional analysis of enzymes required for precorrin-2 dehydrogenation and metal ion insertion in the biosynthesis of sirohaem and cobalamin in Bacillus megaterium
Biochem. J.
370
505-516
2003
Priestia megaterium (P61818), Priestia megaterium, Priestia megaterium DSM 509 (P61818)
Manually annotated by BRENDA team
Schubert, H.L.; Rose, R.S.; Leech, H.K.; Brindley, A.A.; Hill, C.P.; Rigby, S.E.; Warren, M.J.
Structure and function of SirC from Bacillus megaterium - a metal binding precorrin-2 dehydrogenase
Biochem. J.
415
257-263
2008
Priestia megaterium (P61818), Priestia megaterium
Manually annotated by BRENDA team