Information on EC 1.14.13.83 - precorrin-3B synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.83
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RECOMMENDED NAME
GeneOntology No.
precorrin-3B synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
precorrin-3A + NADH + H+ + O2 = precorrin-3B + NAD+ + H2O
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
cob(II)yrinate a,c-diamide biosynthesis II (late cobalt incorporation)
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vitamin B12 metabolism
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Porphyrin and chlorophyll metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
precorrin-3A,NADH:oxygen oxidoreductase (20-hydroxylating)
An iron-sulfur protein. An oxygen atom from dioxygen is incorporated into the macrocycle at C-20. In the aerobic cobalamin biosythesis pathway, four enzymes are involved in the conversion of precorrin-3A to precorrin-6A. The first of the four steps is carried out by EC 1.14.13.83, precorrin-3B synthase (CobG), yielding precorrin-3B as the product. This is followed by three methylation reactions, which introduce a methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM; EC 2.1.1.133) and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving rise to precorrin-4, precorrin-5 and precorrin-6A, respectively.
CAS REGISTRY NUMBER
COMMENTARY hide
152787-63-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 16 M
SwissProt
Manually annotated by BRENDA team
strain 16 M
SwissProt
Manually annotated by BRENDA team
strain G3575
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Manually annotated by BRENDA team
strain SC510 (RifT)
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Manually annotated by BRENDA team
in bacteria such as Rhodobacter capsulatus CobG is substituted by an isofunctional protein called CobZ
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
precorrin-3 + NADH + H+ + O2
precorrin-3x + NAD+ + H2O
show the reaction diagram
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
show the reaction diagram
precorrin-3A + NADH + H+ + O2
precorrrin-3B + NAD+ + H2O
show the reaction diagram
precorrin-3A + NADH + O2
precorrin-3B + NAD+ + H2O
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
precorrin-3 + NADH + H+ + O2
precorrin-3x + NAD+ + H2O
show the reaction diagram
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biosynthesis of vitamin B12, part of the ring contractase system for oxidative ring contraction
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ir
precorrin-3A + NADH + H+ + O2
precorrin-3B + NAD+ + H2O
show the reaction diagram
precorrin-3A + NADH + H+ + O2
precorrrin-3B + NAD+ + H2O
show the reaction diagram
precorrin-3A + NADH + O2
precorrin-3B + NAD+ + H2O
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
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enzyme-bound
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe-S center
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
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SDS-PAGE
46690
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calculated from the gene sequence
46990
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predicted from the DNA sequence
48000
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SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
upon handling or storing CobG preparations, the sulfur content, the A400, and the enzymatic activity drops simultaneously
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
centrifugation of cells, pellet resuspended in binding buffer (20 mM Tris-HCl, pH 8.0, containing 0.5 M NaCl and 5 mM imidazole), cells broken up with a cell disrupter or sonicated, centrifugation, supernatant transferred to an anaerobic glove box, applied to a metal affinity chromatography column charged with Ni2+, washed with buffer with 20 mM imidazole, elution with 400 mM imidazole
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Brucella melitensis cobG is PCR-amplified, overexpression of recombinant enzyme in Escherichia coli BL21 (DE3) inducible with isopropyl-1-thio-beta-D-galactopyranoside
expressed in Escherichia coli BL21DE3
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gene cobG heterologously expressed in Escherichia coli
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genetic and sequence analysis
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overexpressed in recombinant strains of Escherichia coli
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Pseudomonas denitrificans cobG is PCR-amplified in plasmid pCR427 and cloned into pET14b, overexpression of recombinant enzyme in Escherichia coli BL21 (DE3) inducible with isopropyl-1-thio-beta-D-galactopyranoside
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C358A
no activity, no Fe-S center
C364A
no activity, no Fe-S center
C394A
no activity, no Fe-S center
C398A
no activity, no Fe-S center
C42A
active, Fe-S center present
H390A
active, Fe-S center present
C358A
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no activity, no Fe-S center
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C364A
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no activity, no Fe-S center
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C394A
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no activity, no Fe-S center
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C42A
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active, Fe-S center present
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C358A
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no activity, no Fe-S center
C364A
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no activity, no Fe-S center
C394A
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no activity, no Fe-S center
C398A
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no activity, no Fe-S center
C42A
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active, Fe-S center present
H390A
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active, Fe-S center present
additional information
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