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show all sequences of 4.6.1.17

Structural insights into putative molybdenum cofactor biosynthesis protein C (MoaC2) from Mycobacterium tuberculosis H37Rv

Srivastava, V.K.; Srivastava, S.; Srivastava, S.; Arora, A.; Pratap, J.V.; PLoS ONE 8, e58333 (2013)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
purified recombinant MoaC2s in apo form, X-ray diffraction structure determination and analysis at 2.2-2.5 A resolution
Mycobacterium tuberculosis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
17500
-
2 * 17500, MoaC2 functional form
Mycobacterium tuberculosis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
GTP
Mycobacterium tuberculosis
-
cyclic pyranopterin phosphate + diphosphate
-
-
?
GTP
Mycobacterium tuberculosis H37Rv
-
cyclic pyranopterin phosphate + diphosphate
-
-
?
additional information
Mycobacterium tuberculosis
the GTP molecule first binds to MoaA and an intermediate formamidopyrimidine-type compound is generated which is subsequently used by MoaC. MoaC catalyzes the release of diphosphate from the formamidopyrimidine-type compound and the formation of the cyclic phosphate of precursor Z, which is formed either via the formation of intermediate compound E (formamido-type) or PBM (pteridinebenzomonophosphate)
?
-
-
-
additional information
Mycobacterium tuberculosis H37Rv
the GTP molecule first binds to MoaA and an intermediate formamidopyrimidine-type compound is generated which is subsequently used by MoaC. MoaC catalyzes the release of diphosphate from the formamidopyrimidine-type compound and the formation of the cyclic phosphate of precursor Z, which is formed either via the formation of intermediate compound E (formamido-type) or PBM (pteridinebenzomonophosphate)
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Mycobacterium tuberculosis
P9WJR7
MoaC2; gene Rv0864
-
Mycobacterium tuberculosis H37Rv
P9WJR7
MoaC2; gene Rv0864
-
Reaction
Reaction
Commentary
Organism
GTP = cyclic pyranopterin phosphate + diphosphate
mechanisms proposed for the first step of the Moco biosynthesis pathway, overview
Mycobacterium tuberculosis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
GTP
-
728595
Mycobacterium tuberculosis
cyclic pyranopterin phosphate + diphosphate
-
-
-
?
GTP
-
728595
Mycobacterium tuberculosis H37Rv
cyclic pyranopterin phosphate + diphosphate
-
-
-
?
additional information
the GTP molecule first binds to MoaA and an intermediate formamidopyrimidine-type compound is generated which is subsequently used by MoaC. MoaC catalyzes the release of diphosphate from the formamidopyrimidine-type compound and the formation of the cyclic phosphate of precursor Z, which is formed either via the formation of intermediate compound E (formamido-type) or PBM (pteridinebenzomonophosphate)
728595
Mycobacterium tuberculosis
?
-
-
-
-
additional information
molecular docking studies with probable ligands suggests that pteridinebenzomonophosphate is the most likely ligand. Molybdenum cofactor biosynthesis protein A1, MoaA1, and MoaC2 interact with each other in a complex and do not act independently of each other, homology modeling of MoaA1 complexed with MoaC2 and protein-protein interaction analysis, detailed docking study, overview
728595
Mycobacterium tuberculosis
?
-
-
-
-
additional information
the GTP molecule first binds to MoaA and an intermediate formamidopyrimidine-type compound is generated which is subsequently used by MoaC. MoaC catalyzes the release of diphosphate from the formamidopyrimidine-type compound and the formation of the cyclic phosphate of precursor Z, which is formed either via the formation of intermediate compound E (formamido-type) or PBM (pteridinebenzomonophosphate)
728595
Mycobacterium tuberculosis H37Rv
?
-
-
-
-
additional information
molecular docking studies with probable ligands suggests that pteridinebenzomonophosphate is the most likely ligand. Molybdenum cofactor biosynthesis protein A1, MoaA1, and MoaC2 interact with each other in a complex and do not act independently of each other, homology modeling of MoaA1 complexed with MoaC2 and protein-protein interaction analysis, detailed docking study, overview
728595
Mycobacterium tuberculosis H37Rv
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
2 * 17500, MoaC2 functional form
Mycobacterium tuberculosis
hexamer
MoaC2 mainly forms hexamers, which are not functional
Mycobacterium tuberculosis
More
tertiary and quaternary structures of MoaC2, detailed overview
Mycobacterium tuberculosis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant MoaC2s in apo form, X-ray diffraction structure determination and analysis at 2.2-2.5 A resolution
Mycobacterium tuberculosis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
17500
-
2 * 17500, MoaC2 functional form
Mycobacterium tuberculosis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
GTP
Mycobacterium tuberculosis
-
cyclic pyranopterin phosphate + diphosphate
-
-
?
GTP
Mycobacterium tuberculosis H37Rv
-
cyclic pyranopterin phosphate + diphosphate
-
-
?
additional information
Mycobacterium tuberculosis
the GTP molecule first binds to MoaA and an intermediate formamidopyrimidine-type compound is generated which is subsequently used by MoaC. MoaC catalyzes the release of diphosphate from the formamidopyrimidine-type compound and the formation of the cyclic phosphate of precursor Z, which is formed either via the formation of intermediate compound E (formamido-type) or PBM (pteridinebenzomonophosphate)
?
-
-
-
additional information
Mycobacterium tuberculosis H37Rv
the GTP molecule first binds to MoaA and an intermediate formamidopyrimidine-type compound is generated which is subsequently used by MoaC. MoaC catalyzes the release of diphosphate from the formamidopyrimidine-type compound and the formation of the cyclic phosphate of precursor Z, which is formed either via the formation of intermediate compound E (formamido-type) or PBM (pteridinebenzomonophosphate)
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
GTP
-
728595
Mycobacterium tuberculosis
cyclic pyranopterin phosphate + diphosphate
-
-
-
?
GTP
-
728595
Mycobacterium tuberculosis H37Rv
cyclic pyranopterin phosphate + diphosphate
-
-
-
?
additional information
the GTP molecule first binds to MoaA and an intermediate formamidopyrimidine-type compound is generated which is subsequently used by MoaC. MoaC catalyzes the release of diphosphate from the formamidopyrimidine-type compound and the formation of the cyclic phosphate of precursor Z, which is formed either via the formation of intermediate compound E (formamido-type) or PBM (pteridinebenzomonophosphate)
728595
Mycobacterium tuberculosis
?
-
-
-
-
additional information
molecular docking studies with probable ligands suggests that pteridinebenzomonophosphate is the most likely ligand. Molybdenum cofactor biosynthesis protein A1, MoaA1, and MoaC2 interact with each other in a complex and do not act independently of each other, homology modeling of MoaA1 complexed with MoaC2 and protein-protein interaction analysis, detailed docking study, overview
728595
Mycobacterium tuberculosis
?
-
-
-
-
additional information
the GTP molecule first binds to MoaA and an intermediate formamidopyrimidine-type compound is generated which is subsequently used by MoaC. MoaC catalyzes the release of diphosphate from the formamidopyrimidine-type compound and the formation of the cyclic phosphate of precursor Z, which is formed either via the formation of intermediate compound E (formamido-type) or PBM (pteridinebenzomonophosphate)
728595
Mycobacterium tuberculosis H37Rv
?
-
-
-
-
additional information
molecular docking studies with probable ligands suggests that pteridinebenzomonophosphate is the most likely ligand. Molybdenum cofactor biosynthesis protein A1, MoaA1, and MoaC2 interact with each other in a complex and do not act independently of each other, homology modeling of MoaA1 complexed with MoaC2 and protein-protein interaction analysis, detailed docking study, overview
728595
Mycobacterium tuberculosis H37Rv
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 17500, MoaC2 functional form
Mycobacterium tuberculosis
hexamer
MoaC2 mainly forms hexamers, which are not functional
Mycobacterium tuberculosis
More
tertiary and quaternary structures of MoaC2, detailed overview
Mycobacterium tuberculosis
Other publictions for EC 4.6.1.17
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
739551
Hover
Mechanism of pyranopterin ring ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
112
6347-6352
2015
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8
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6
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1
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1
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5
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8
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6
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1
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5
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1
1
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747097
Hover
Mechanistic investigation of ...
Escherichia coli
Biochemistry
54
7229-7236
2015
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1
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1
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1
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1
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1
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728595
Srivastava
Structural insights into putat ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
PLoS ONE
8
e58333
2013
-
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1
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1
4
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6
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1
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6
3
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1
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1
4
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6
3
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-
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726621
Srivastava
Overexpression, purification, ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Acta Crystallogr. Sect. F
68
687-691
2012
-
-
1
1
-
-
-
-
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-
1
2
-
6
-
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1
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2
1
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1
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1
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1
2
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1
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2
1
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713617
Kanaujia
Structures of apo and GTP-boun ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Acta Crystallogr. Sect. D
66
821-833
2010
1
-
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1
-
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90
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1
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2
1
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1
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1
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2
1
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713624
Yoshida
Structure of a putative molybd ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7
Acta Crystallogr. Sect. F
64
589-592
2008
1
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1
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5
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2
1
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2
1
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739638
Gray
Diverse splicing mechanisms fu ...
Homo sapiens
RNA
6
928-936
2000
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1
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1
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714888
Rieder
Rearrangement reactions in the ...
Escherichia coli
Eur. J. Biochem.
255
24-36
1998
-
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1
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1
1
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715420
Wuebbens
Investigation of the early ste ...
Escherichia coli
J. Biol. Chem.
270
1082-1087
1995
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