Information on EC 1.97.1.9 - selenate reductase

for references in articles please use BRENDA:EC1.97.1.9
Word Map on EC 1.97.1.9
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.97.1.9
-
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
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Selenocompound metabolism
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from Sabzevar of Iran
-
-
Manually annotated by BRENDA team
isolated from Sabzevar of Iran
-
-
Manually annotated by BRENDA team
isolated from sediment layer of seven locations on two mine sites, one near the town of Likely in British Columbia, Canada and the other in the Elk Valley in British Columbia, Canada
-
-
Manually annotated by BRENDA team
isolated from sediment layer of seven locations on two mine sites, one near the town of Likely in British Columbia, Canada and the other in the Elk Valley in British Columbia, Canada
-
-
Manually annotated by BRENDA team
isolated from sediment layer of seven locations on two mine sites, one near the town of Likely in British Columbia, Canada and the other in the Elk Valley in British Columbia, Canada
-
-
Manually annotated by BRENDA team
isolated from sediment layer of seven locations on two mine sites, one near the town of Likely in British Columbia, Canada and the other in the Elk Valley in British Columbia, Canada
UniProt
Manually annotated by BRENDA team
isolated from sediment layer of seven locations on two mine sites, one near the town of Likely in British Columbia, Canada and the other in the Elk Valley in British Columbia, Canada
UniProt
Manually annotated by BRENDA team
isolated from sediment layer of seven locations on two mine sites, one near the town of Likely in British Columbia, Canada and the other in the Elk Valley in British Columbia, Canada
-
-
Manually annotated by BRENDA team
alpha, beta, and gamma subunits serA, serB, and serC of selenate reductase; from selenate-reducing membrane biofilm reactor (MBfR) biofilms
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isolated from sediment layer of seven locations on two mine sites, one near the town of Likely in British Columbia, Canada and the other in the Elk Valley in British Columbia, Canada
-
-
Manually annotated by BRENDA team
isolated from sediment layer of seven locations on two mine sites, one near the town of Likely in British Columbia, Canada and the other in the Elk Valley in British Columbia, Canada
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
activity of genes iscU or hscB in the Isc iron-sulfur cluster biosynthesis pathway is required for formation of selenate reductase activity in vivo. Mutant strains JW2513 and JW2511 devoid of either the iscU or hscB gene in the Isc iron–sulfur cluster biosynthesis pathway lose the ability to reduce selenate, phenotypes, overview. Genetic complementation by the wildtype sequences restored selenate reductase activity. The Isc biosynthetic system plays a key role in selenate reductase Fe-S cofactor assembly and is essential for enzyme activity
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
selenate + acetate
selenite + H2O + CO2
show the reaction diagram
-
-
-
?
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
-
-
-
-
?
selenate + H2
selenite + H2O
show the reaction diagram
-
-
-
-
?
selenate + lactate
selenite + H2O + acetate + HCO3-
show the reaction diagram
selenate + malate
?
show the reaction diagram
-
-
-
-
?
selenate + NADH + H+
selenite + H2O + NAD+
show the reaction diagram
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
-
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
-
-
?
selenate + reduced methyl viologen
selenite + H2O + methyl viologen
show the reaction diagram
-
-
-
-
?
selenate + reduced methyl viologen
selenite + H2O + oxidized methyl viologen
show the reaction diagram
selenite + NADH + H+
selenium + H2O + NAD+
show the reaction diagram
additional information
?
-
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 + NADH + H+
selenite + H2O + NAD+
show the reaction diagram
selenate + reduced acceptor
selenite + H2O + acceptor
show the reaction diagram
selenite + NADH + H+
selenium + H2O + NAD+
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome b
-
iron-sulfur center
-
activity of genes iscU or hscB in the Isc iron-sulfur cluster biosynthesis pathway is required for formation of selenate reductase activity in vivo
iron-sulfur centre
-
at least 2 [Fe-S]-centre as prosthetic groups per enzyme molecule
molybdopterin
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mo2+
-
role of Mo2+ in selenate reductase
Molybdenum
Non-heme iron
-
-
selenium
-
isolated enzyme contains a reduced form of selenium, probably as selenocysteine
sulfur
-
iron-sulfur centre
additional information
-
Na+ and Mg2+ have no effect on the activity at 1 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
-
70% inhibition at 1 mM
Ca2+
-
about 20% inhibition at 1 mM
EDTA
-
inhibits the enzymatic reducing activity slightly, addition of Mo2+ and Zn2+ to the reaction mixture eliminates the EDTA inhibitory effect
Hg2+
-
complete inhibition at 1 mM
Mn2+
-
35% inhibition at 1 mM
N-ethyl maleimide
-
complete inhibition
NaN3
-
60% inhibition at 1 mM
Pb2+
-
45% inhibition at 1 mM
selenate
-
mixed-type inhibition
Thiocyanate
-
mixed-type inhibition
tungstate
Zn2+
-
30% inhibition at 1 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
selenate
-
induction of enzyme activity when included in growth medium
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.25
benzyl viologen
-
20°C
0.0007 - 6.25
selenate
5.47
Selenite
-
pH 6.0, 35°C
additional information
additional information
-
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
-
30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.29
-
membrane fraction
0.76
-
wild-type, cells grown on nitrate
1.6
-
wild-type, cells grown on selenate + nitrate
3.84
-
wild-type, cells grown on selenate
15.36
-
purified enzyme, pH 6.0, 35°C
41.4
-
purified enzyme
500
-
pH 7.2, 30°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
activity range, profile overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
in vivo assay at
65
-
optimal temperature for molybdenum-SER
80
-
optimal temperature for tungsten-SER is higher than 80°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 70
-
activity range, profile overview, 70% and 35% of maximum activity at 50°C and 60°C
additional information
-
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
21000
-
alphabetagammadelta, 1 * 82000 + 1 * 53000 + 1 * 34000 + 1 * 21000
34000
-
alphabetagammadelta, 1 * 82000 + 1 * 53000 + 1 * 34000 + 1 * 21000
36000
-
3* 100, alpha-subunit, 3 * 55000, beta-subunit, 3 * 36000, gamma-subunit, SDS-PAGE
37000
-
1 * 99000, alpha, + 1 * 37000, beta, + 1 * 23000, gamma, SDS-PAGE
55000
-
3* 100, alpha-subunit, 3 * 55000, beta-subunit, 3 * 36000, gamma-subunit, SDS-PAGE
99000
-
1 * 99000, alpha, + 1 * 37000, beta, + 1 * 23000, gamma, SDS-PAGE
180000
197000
-
gel filtration
600000
-
gel filtration
700000
-
native gel electrophoresis of cell-free extracts and activity stain
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
heterotrimer
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
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
purified molybdenum-SER complex is stable and active upon heat-shock incubation for 10 min at temperatures up to 60°C. At temperatures greater than 65°C all three subunits (SerABC) are readily denatured
additional information
-
thermal stability analysis by differential scanning calorim
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Methanol
n-propanol
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, enzyme extracted with Thesit retains 50% activity after being frozen for prolonged periods
-
4°C, enzyme extracted with Thesit remains active for 24 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
57fold, to near homogeneity
-
native enzyme 21.29fold by ammonium sulfate fractionation, anion exchange and hydrophonic interaction chromatography, followed by ultrafiltration
-
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
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
gene serA, DNA and amino acid sequence determination and analysis, phylogenetic analysis, quantitative PCR expression analysis
gene serA, quantitative PCR expression analysis
gene ynfE, encoded by the ynfEFGH-dmsD operon, the YnfE protein is synthesized with an N-terminal twin-arginine signal peptide and biosynthesis of the enzyme is coordinated by a signal peptide binding chaperone called DmsD
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A28Q
-
site-directed mutagenesis, the mutant is devoid of selenate reductase activity and can be rescued by providing chaperon protein DmsD in excess
F35Q
-
site-directed mutagenesis
L24Q
-
site-directed mutagenesis, the mutant is devoid of selenate reductase activity
L33Q
-
site-directed mutagenesis, the mutant is still able to correctly assemble selenate reductase
V31Q
-
site-directed mutagenesis
A28Q
-
site-directed mutagenesis, the mutant is devoid of selenate reductase activity and can be rescued by providing chaperon protein DmsD in excess
-
F35Q
-
site-directed mutagenesis
-
L24Q
-
site-directed mutagenesis, the mutant is devoid of selenate reductase activity
-
L33Q
-
site-directed mutagenesis, the mutant is still able to correctly assemble selenate reductase
-
V31Q
-
site-directed mutagenesis
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
environmental protection
Show AA Sequence (109 entries)
Please use the Sequence Search for a specific query.