BRENDA - Enzyme Database show
show all sequences of 1.20.99.1

Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 A and 2.03 A

Ellis, P.J.; Conrads, T.; Hille, R.; Kuhn, P.; Structure 9, 125-132 (2001)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
induction by arsenite
Alcaligenes faecalis
Crystallization (Commentary)
Crystallization
Organism
X-ray diffraction structure determination and analysis of 2 different crystal forms at 1.64-2.03 A using multiple isomorphous replacement with anomalous scattering and multiple-wavelength anomalous dispersion methods
Alcaligenes faecalis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron
enzyme is a MoFe protein, Mo atom bound to 2 pterin cofactors and a [3Fe4S] cluster, binding site on the large subunit, the small subunit contains a binding site for a Rieske-type [2Fe2S] cluster
Alcaligenes faecalis
Molybdenum
enzyme is a MoFe protein, Mo atom bound to 2 pterin cofactors and a [3Fe4S] cluster, binding site on the large subunit, the Mo atom is not covalently bound to the polypeptide
Alcaligenes faecalis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
arsenite + acceptor
Alcaligenes faecalis
detoxification of arsenite to the less toxic arsenate prior to methylation
arsenate + reduced acceptor
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Alcaligenes faecalis
-
NCIB 8687
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
arsenite + acceptor
-
287858
Alcaligenes faecalis
arsenate + reduced acceptor
-
-
-
?
arsenite + acceptor
detoxification of arsenite to the less toxic arsenate prior to methylation
287858
Alcaligenes faecalis
arsenate + reduced acceptor
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
large subunit of 825 amino acid residues and a small subunit of 134 amino acid residues
Alcaligenes faecalis
Cofactor
Cofactor
Commentary
Organism
Structure
Pterin molybdenum cofactor
enzyme is a MoFe protein, Mo atom bound to 2 pterin cofactors and a [3Fe4S] cluster, binding site on the large subunit
Alcaligenes faecalis
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
induction by arsenite
Alcaligenes faecalis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
Pterin molybdenum cofactor
enzyme is a MoFe protein, Mo atom bound to 2 pterin cofactors and a [3Fe4S] cluster, binding site on the large subunit
Alcaligenes faecalis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
X-ray diffraction structure determination and analysis of 2 different crystal forms at 1.64-2.03 A using multiple isomorphous replacement with anomalous scattering and multiple-wavelength anomalous dispersion methods
Alcaligenes faecalis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron
enzyme is a MoFe protein, Mo atom bound to 2 pterin cofactors and a [3Fe4S] cluster, binding site on the large subunit, the small subunit contains a binding site for a Rieske-type [2Fe2S] cluster
Alcaligenes faecalis
Molybdenum
enzyme is a MoFe protein, Mo atom bound to 2 pterin cofactors and a [3Fe4S] cluster, binding site on the large subunit, the Mo atom is not covalently bound to the polypeptide
Alcaligenes faecalis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
arsenite + acceptor
Alcaligenes faecalis
detoxification of arsenite to the less toxic arsenate prior to methylation
arsenate + reduced acceptor
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
arsenite + acceptor
-
287858
Alcaligenes faecalis
arsenate + reduced acceptor
-
-
-
?
arsenite + acceptor
detoxification of arsenite to the less toxic arsenate prior to methylation
287858
Alcaligenes faecalis
arsenate + reduced acceptor
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
large subunit of 825 amino acid residues and a small subunit of 134 amino acid residues
Alcaligenes faecalis
Other publictions for EC 1.20.99.1
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)
744115
Mirza
New arsenate reductase gene ( ...
uncultured bacterium
Appl. Environ. Microbiol.
83
e02725-16
2017
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745908
Salt
Would the real arsenate reduc ...
Arabidopsis thaliana
New Phytol.
215
926-928
2017
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1
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1
1
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744726
Kumari
Genetic identification of ars ...
Escherichia coli, Escherichia coli R773
Chemosphere
163
400-412
2016
2
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2
1
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745124
Chaturvedi
Phylogenetic analysis of gamm ...
Acinetobacter sp., Citrobacter sp., Enterobacter cloacae, Enterobacter sp., Escherichia coli, Hafnia alvei, Klebsiella pneumoniae, Klebsiella sp., Salmonella sp., Serratia sp., Shigella flexneri, Shigella sp., Yersinia sp., Yokenella regensburgei
Interdiscip. Sci.
6
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14
-
14
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14
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14
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14
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745852
Sanchez-Bermejo
Natural variation in arsenate ...
Arabidopsis thaliana
Nat. Commun.
5
4617
2014
-
-
1
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1
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1
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2
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1
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2
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746165
Chao
Genome-wide association mappi ...
Arabidopsis thaliana
PLoS Biol.
12
e1002009
2014
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-
1
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1
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1
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2
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1
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1
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1
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2
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1
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1
2
2
1
-
-
746413
Wu
Prokaryotic arsenate reductas ...
Bacillus subtilis
Recent Pat. Food Nutr. Agric.
6
73-81
2014
-
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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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1
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-
1
-
-
713790
Srivastava
Pentavalent arsenate reductase ...
Pseudomonas sp.
Appl. Biochem. Biotechnol.
162
766-779
2010
4
-
-
-
-
-
-
-
-
4
-
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-
1
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2
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1
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1
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2
1
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4
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4
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2
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1
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1
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2
1
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-
713882
Freikowski
Hydrogen formation by an arsen ...
Pseudomonas putida
Appl. Microbiol. Biotechnol.
88
1363-1371
2010
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1
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1
1
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-
714217
Bhattacharjee
Adventitious arsenate reductas ...
Homo sapiens
Biochemistry
49
802-809
2010
-
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1
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3
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4
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1
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1
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1
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1
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4
1
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1
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3
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4
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1
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1
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1
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4
1
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1
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1
4
4
715880
Jareonmit
Structure and diversity of ars ...
Arthrobacter koreensis, Betaproteobacteria
J. Microbiol. Biotechnol.
20
169-178
2010
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716477
Nagarajan
-
Arsenate reductase activity in ...
Pteris vittata
Plant Biosyst.
144
857-859
2010
2
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1
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2
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1
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1
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696045
Richey
Respiratory arsenate reductase ...
Alkalilimnicola ehrlichii, Alkaliphilus oremlandii, Shewanella sp., Shewanella sp. ANA-3
Biochem. Biophys. Res. Commun.
382
298-302
2009
-
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11
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16
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16
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674785
Li
Conformational fluctuations co ...
Bacillus subtilis
J. Biol. Chem.
282
11078-11083
2007
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1
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693852
Wang
-
Reduction of arsenic oxidative ...
Triticum sp.
J. Plant Nutr.
30
2105-2117
2007
2
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694407
Duan
A CDC25 homologue from rice fu ...
Oryza sativa
New Phytol.
174
311-321
2007
2
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1
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1
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6
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2
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2
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1
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2
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2
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6
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2
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6
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4
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2
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6
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671156
Bisacchi
Crystallization and preliminar ...
Leishmania major
Acta Crystallogr. Sect. F
F62
976-979
2006
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1
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1
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674507
Guo
Solution structures and backbo ...
Bacillus subtilis
J. Biol. Chem.
280
39601-39608
2005
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1
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658052
Hoke
Electrochemical studies of ars ...
Alcaligenes faecalis
Biochemistry
43
1667-1674
2004
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1
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658195
vanden Hoven
Arsenite oxidation by the hete ...
Hydrogenophaga sp. NT14, Hydrogenophaga sp. NT-26
Biochim. Biophys. Acta
1656
148-155
2004
-
-
-
-
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2
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4
6
2
-
2
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1
2
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1
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4
2
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1
1
-
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2
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2
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2
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4
6
2
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1
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1
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4
2
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1
1
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-
-
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660461
DeMel
Arginine 60 in the ArsC arsena ...
Escherichia coli
Protein Sci.
13
2330-2340
2004
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1
2
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1
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1
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1
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658961
Conrads
The active site of arsenite ox ...
Alcaligenes faecalis
J. Am. Chem. Soc.
124
11276-11277
2002
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1
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1
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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
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