Information on EC 1.97.1.9 - selenate reductase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
1.97.1.9
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RECOMMENDED NAME
GeneOntology No.
selenate reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
selenite + H2O + acceptor = selenate + reduced acceptor
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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redox reaction
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-
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reduction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Selenocompound metabolism
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SYSTEMATIC NAME
IUBMB Comments
selenite:reduced acceptor oxidoreductase
The periplasmic enzyme from Thauera selenatis is a complex comprising three heterologous subunits (alpha, beta and gamma) that contains molybdenum, iron, acid-labile sulfide and heme b as cofactor constituents. Nitrate, nitrite, chlorate and sulfate are not substrates. A number of compounds, including acetate, lactate, pyruvate, and certain sugars, amino acids, fatty acids, di- and tricarboxylic acids, and benzoate can serve as electron donors.
CAS REGISTRY NUMBER
COMMENTARY hide
146359-71-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain SLDa-1
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Manually annotated by BRENDA team
genes ygfK, ygfM, and ygfN encode the 3 subunit polypeptides YgfK, YgfM, and YgfN; strain K-12 and derivatives
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Manually annotated by BRENDA team
strain CA5
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Manually annotated by BRENDA team
strain CA5
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Manually annotated by BRENDA team
strain SES-3
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
selenate + acetate
selenite + H2O + CO2
show the reaction diagram
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-
-
?
selenate + electron donor
selenite + H2O + oxidized donor
show the reaction diagram
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
selenate + glucose
?
show the reaction diagram
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-
-
-
?
selenate + H2
selenite + H2O
show the reaction diagram
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-
-
-
?
selenate + lactate
selenite + H2O + acetate + HCO3-
show the reaction diagram
selenate + malate
?
show the reaction diagram
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-
-
-
?
selenate + pyruvate
?
show the reaction diagram
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
selenate + reduced benzyl viologen
selenite + H2O + benzyl viologen
show the reaction diagram
selenate + reduced benzyl viologen
selenite + H2O + oxidized benzyl viologen
show the reaction diagram
selenate + reduced cytc-Ts4
selenite + H2O + oxidized cytc-Ts4
show the reaction diagram
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a c-type cytochrom is purified and shown to donate electrons to SerABC in vitro. Redox potentiometry, combined with UV-visible spectroscopy, show that cytc-Ts4 is a diheme cytochrome with a redox potential of +/-282 mV, and both hemes are predicted to have His-Met ligation
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-
?
selenate + reduced methyl viologen
selenite + H2O + methyl viologen
show the reaction diagram
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-
-
-
?
selenate + reduced methyl viologen
selenite + H2O + oxidized methyl viologen
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
selenate + electron donor
selenite + H2O + oxidized electron donor
show the reaction diagram
selenate + H2
selenite + H2O
show the reaction diagram
-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome b
iron-sulfur centre
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at least 2 [Fe-S]-centre as prosthetic groups per enzyme molecule
molybdopterin
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Molybdenum
Non-heme iron
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selenium
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isolated enzyme contains a reduced form of selenium, probably as selenocysteine
sulfur
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iron-sulfur centre
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
selenate
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mixed-type inhibition
Thiocyanate
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mixed-type inhibition
tungstate
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
selenate
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induction of enzyme activity when included in growth medium
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.25
benzyl viologen
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20C
0.0007 - 6.25
selenate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5 - 387
selenate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.9
Thiocyanate
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30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.29
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membrane fraction
0.42
Q9S1H0 and Q9S1G9 and Q9S1G7
wild-type
0.76
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wild-type, cells grown on nitrate
1.6
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wild-type, cells grown on selenate + nitrate
3.84
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wild-type, cells grown on selenate
41.4
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purified enzyme
500
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pH 7.2, 30C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
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optimal temperature for molybdenum-SER
80
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optimal temperature for tungsten-SER is higher than 80C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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maximal growth at a pH range of pH 9.0-11.0
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
180000
600000
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gel filtration
700000
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native gel electrophoresis of cell-free extracts and activity stain
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nonamer
tetramer
trimer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion method, precipitation by ammonium sulfate, protein solution: 10 mg/ml, 0.3-0.5 M ammonium sulfate, 50 mM piperazine, pH 6.0, reservoir solution: 1.8-2.2 M ammonium sulfate, 100 mM Tris-HCl, pH 8.0-8.9, 293 K, 2-4 weeks, cryoprotection by 25% glycerol, X-ray structure determination and analysis
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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purified molybdenum-SER complex is stable and active upon heat-shock incubation for 10 min at temperatures up to 60C. At temperatures greater than 65C all three subunits (SerABC) are readily denatured
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, enzyme extracted with Thesit retains 50% activity after being frozen for prolonged periods
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4C, enzyme extracted with Thesit remains active for 24 h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
57fold, to near homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, contruction of gene bank, genomic organisationand potential function of: genes serA, serB, and serC, additional overlapping serD
Q9S1H0 and Q9S1G9 and Q9S1G7
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information