BRENDA - Enzyme Database show
show all sequences of 7.3.2.7

Functional promiscuity of homologues of the bacterial ArsA ATPases

Castillo, R.; Saier, M.H.; Int. J. Microbiol. 2010, 187373 (2010)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
ArsD
ArsD is a metallochaperone which sequesters arsenite and antimonite and transfers them to the ArsA ATPase increasing the apparent affinity of ArsA for its substrates and lowering the concentration of free As(III) and Sb(III) in the cytosol
Escherichia coli
Cloned(Commentary)
Commentary
Organism
gene arsA, phylogenetic analysis with detailed analysis of clustering in the superfamily, overview
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + H2O + antimonite/in
Escherichia coli
-
ADP + phosphate + antimonite/out
-
-
-
ATP + H2O + arsenite/in
Escherichia coli
-
ADP + phosphate + arsenite/out
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
genes arsA and arsB
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + H2O + antimonite/in
-
719612
Escherichia coli
ADP + phosphate + antimonite/out
-
-
-
-
ATP + H2O + arsenite/in
-
719612
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
-
Subunits
Subunits
Commentary
Organism
More
subunit ArsA exhibuts ATPase activity and subunit ArsB is a 12 alpha-helix transmembrane spanning pump extruding As(III) and Sb(III)
Escherichia coli
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
ArsD
ArsD is a metallochaperone which sequesters arsenite and antimonite and transfers them to the ArsA ATPase increasing the apparent affinity of ArsA for its substrates and lowering the concentration of free As(III) and Sb(III) in the cytosol
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
gene arsA, phylogenetic analysis with detailed analysis of clustering in the superfamily, overview
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + H2O + antimonite/in
Escherichia coli
-
ADP + phosphate + antimonite/out
-
-
-
ATP + H2O + arsenite/in
Escherichia coli
-
ADP + phosphate + arsenite/out
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + H2O + antimonite/in
-
719612
Escherichia coli
ADP + phosphate + antimonite/out
-
-
-
-
ATP + H2O + arsenite/in
-
719612
Escherichia coli
ADP + phosphate + arsenite/out
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
subunit ArsA exhibuts ATPase activity and subunit ArsB is a 12 alpha-helix transmembrane spanning pump extruding As(III) and Sb(III)
Escherichia coli
General Information
General Information
Commentary
Organism
evolution
phylogenetic analysis of gene arsA and prokaryotic and eukaryotic ArsA homologues with detailed analysis of clustering in the superfamily, overview
Escherichia coli
physiological function
subunit ArsA exhibuts ATPase activity and subunit ArsB is a 12 alpha-helix transmembrane spanning pump extruding As(III) and Sb(III). Transport via ArsB can be energized by the pmf or by forming an oxyanion translocating complex with the catalytic ArsA subunit, coupling ATP hydrolysis to efflux
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
evolution
phylogenetic analysis of gene arsA and prokaryotic and eukaryotic ArsA homologues with detailed analysis of clustering in the superfamily, overview
Escherichia coli
physiological function
subunit ArsA exhibuts ATPase activity and subunit ArsB is a 12 alpha-helix transmembrane spanning pump extruding As(III) and Sb(III). Transport via ArsB can be energized by the pmf or by forming an oxyanion translocating complex with the catalytic ArsA subunit, coupling ATP hydrolysis to efflux
Escherichia coli
Other publictions for EC 7.3.2.7
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)
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A 3D localized surface plasmon ...
Escherichia coli
Biosens. Bioelectron.
38
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733712
Sri Lakshmi Sunita
Molecular identification of ar ...
uncultured bacterium
Ecotoxicology
21
202-212
2012
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719037
Ajees
The ArsD As(III) metallochaper ...
Escherichia coli
Biometals
24
391-399
2011
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715567
Wu
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285
40081-40087
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5
5
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718867
Fu
Role of signature lysines in t ...
Escherichia coli, Escherichia coli JM109
Biochemistry
49
356-364
2010
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31
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4
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718868
Yang
Arsenic binding and transfer b ...
Escherichia coli
Biochemistry
49
3658-3666
2010
2
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Ye
The 1.4 A crystal structure of ...
Saccharomyces cerevisiae
Biochemistry
49
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1
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Biochemical characterization o ...
Alkaliphilus metalliredigens
FEBS Lett.
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719612
Castillo
Functional promiscuity of homo ...
Escherichia coli
Int. J. Microbiol.
2010
187373
2010
1
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2
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697072
Hemmingsson
ASNA1, an ATPase targeting tai ...
Homo sapiens
Cancer Chemother. Pharmacol.
63
491-499
2009
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689052
Ruan
Characterization of the metall ...
Escherichia coli
Mol. Microbiol.
67
392-402
2008
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4
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695985
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Functional participation of a ...
Escherichia coli
Biochem. Biophys. Res. Commun.
368
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2008
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Bhattacharjee
Role of conserved aspartates i ...
Escherichia coli
Biochemistry
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2008
2
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Chang
Biogeochemical cyclic activity ...
Pseudomonas putida
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2008
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687482
Lin
ArsD: an As(III) metallochaper ...
Escherichia coli
J. Bioenerg. Biomembr.
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453-458
2007
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687554
Lin
ArsD residues Cys12, Cys13, an ...
Escherichia coli
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2007
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669530
Ruan
Cys-113 and Cys-422 form a hig ...
Escherichia coli, Escherichia coli plasmid R773
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281
9925-9934
2006
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689739
Lin
An arsenic metallochaperone fo ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
103
15617-15622
2006
1
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656054
Zhou
Unisite and multisite catalysi ...
Escherichia coli
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277
23815-23820
2002
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