Information on EC 3.6.3.29 - molybdate-transporting ATPase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.6.3.29
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RECOMMENDED NAME
GeneOntology No.
molybdate-transporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + molybdate/out = ADP + phosphate + molybdate/in
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (molybdate-importing)
ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports molybdate anions.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
soil isolate, strain 5A
SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain USDA110
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Manually annotated by BRENDA team
genes modABC, organized in the ModABC operon
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Manually annotated by BRENDA team
genes modABC, organized in the ModABC operon
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Manually annotated by BRENDA team
strain DSM3953
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Manually annotated by BRENDA team
strain DSM3953
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
pv. citri, modABC operon
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
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during growth under Mo-replete conditions, the wild-type strain accumulates considerably more Mo than the enzyme mutant
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + chromate/out
?
show the reaction diagram
ATP + H2O + molybdate/out
?
show the reaction diagram
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
show the reaction diagram
ATP + H2O + tungstate/out
?
show the reaction diagram
ATP + H2O + tungsten/out
ADP + phosphate + tungsten/in
show the reaction diagram
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?
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
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molybdate
specific binding of tungstate or molybdate, involving residues Ser286, Thr320, Ser323, and Lys340, to the two oxyanion pockets at the shared interface of the enzyme subunits prevents ATPase activity and locks the enzyme in the inward-facing conformation, with the actives sites of the nucleotide-binding subunits separated. The allosteric effect prevents the transporter from switchuing between the inward-facing and outward-facing states, thus interfering with the access and release mechanism, overview
Tungsten
specific binding of tungstate or molybdate, involving residues Ser286, Thr320, Ser323, and Lys340, to the two oxyanion pockets at the shared interface of the enzyme subunits prevents ATPase activity and locks the enzyme in the inward-facing conformation, with the actives sites of the nucleotide-binding subunits separated. The allosteric effect prevents the transporter from switchuing between the inward-facing and outward-facing states, thus interfering with the access and release mechanism, overview
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ModE
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represses molybdenum transport in presence of both molybdenum and tungsten
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vanadate
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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MOT1 expression in roots is slightly but significantly reduced under Mo limitation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00002
molybdate
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0.000045 - 0.048
MoO42-
additional information
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6
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with molybdate
7
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without molybdate
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOT1 contains an N-terminal mitochondrial targeting sequence
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8100
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6 * 8100, SDS-PAGE, recombinant enzyme
29000
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x * 29000, recombinant enzyme, SDS-PAGE
48000
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gel filtration, native enzyme
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
homohexamer
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
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binding protein ModA of the molybdate transport system is a lipoprotein
no modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ModA/WtpA molybdate- or tungstate-binding protein crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds
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ModA crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds
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ModA with molybdate
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ModA crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds
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ModA with molybdate
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MolA bound to tungstate and molybdate, X-ray diffraction structure determination and analysis at 1.6 A resolution
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enzyme in trans-inhibited state, X-ray diffraction structure determination and analysis at A resolution
ModA in the apoprotein conformation and in the molybdate-bound conformation, by sitting-drop and hanging-drop vapor-diffusion methods, mixing of 0.001 ml of protein solution containing 16-23 mg/ml protein with 0.001 ml reservoir solution, containing 1.4 M ammonium citrate pH 6.4 or 1.4 M ammonium citrate pH 6.0, 4 mM sodium sulfate for the apo-protein and 2.1 M ammonium sulfate and either 1% v/v or 3% v/v 2-propanol, and 4% v/v 2.4 M ammonium sulfate for the molybdate-bound protein, equilibration against 100 ml reservoir solution at room temperature for apo-odA and at 293 K for molybdate-bound ModA, 1 week, method optimization, X-ray diffraction structure determination and analysis of apo- and molybdate-bound-ModA at 1.95 A and 1.69 A resolution and at 2.25 A and 2.45 A resolutionm, respectively, molecular replacemen fails, usage of heavy metal labeling instead
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ModA/WtpA molybdate- or tungstate-binding protein crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds
ModA crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by affinity chromatography
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recombinant His-tagged ModA from Escherichia coli strain BL21-Gold (DE3) by nickel affinity chromatography and gel filtration
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recombinant MolA by affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli DY380 cells
expression of His-tagged ModA in Escherichia coli strain BL21-Gold (DE3)
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expression of His-tagged ModC in Escherichia coli strain BL21(DE3)
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gene molA, recombinant expression
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gene mot1, quantitative expression analysis by RT-PCR, expression of GFP-tagged MOT1 in Nicotiana tabacum BY-2 cells under control of the cauliflower mosaic virus 35S RNA promoter near or at the plasma membrane of BY2 cells
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genotyping, expression in protoplast mitochondrial membranes as GFP-tagged protein, quantitative expression analysis by realtime PCR, expression of MOT1 specifically enhances molybdenum accumulation in Saccharomyces cerevisiae by 5fold
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modA, genetic regulation of tupA/tupB and modA, overview
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overexpressed in Escherichia coli XL 1-Blue as a C-terminal Strep-tag fusion protein
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activation of modA and modBC genes by TunR in Desulfovibrio vulgaris in vivo; activation of modA and modBC genes by TunR in Desulfovibrio vulgaris in vivo; activation of modA and modBC genes by TunR in Desulfovibrio vulgaris in vivo
expression of perO is independent of molybdate and sulfate availabilities
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genetic regulation of tupA and modA, overview
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ModC is negatively regulated by the transcription factors MopA and MopB, overview. MopB negatively modulates expression of the mop promoter, and formation of MopA-MopB heteromers, independent of Mo availability, might represent a fine-tuning mechanism controlling mop gene expression. Oligomerization and Mo-binding properties of MopA and MopB, overview
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the periplasmic protein involved in molybdate transport, ModA, is downregulated under high molybdate concentration stress conditions
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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