We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments 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.
The taxonomic range for the selected organisms is: Thauera selenatis The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
selenate reductase, serabc,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
selenate reductase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
selenite + H2O + acceptor = selenate + reduced acceptor
electron transport mechanism
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
selenate + acetate
selenite + H2O + CO2
-
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
selenate + glucose
?
-
-
-
-
?
selenate + H2
selenite + H2O
-
-
-
-
?
selenate + lactate
selenite + H2O + acetate + HCO3-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
selenate + reduced benzyl viologen
selenite + H2O + oxidized benzyl viologen
selenate + reduced cytc-Ts4
selenite + H2O + oxidized cytc-Ts4
-
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 + oxidized methyl viologen
additional information
?
-
selenate + electron donor
selenite + H2O + oxidized electron donor
-
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
-
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
-
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
-
specific for selenate
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
-
specific for selenate
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
-
-
-
?
selenate + reduced benzyl viologen
selenite + H2O + oxidized benzyl viologen
-
-
-
-
?
selenate + reduced benzyl viologen
selenite + H2O + oxidized benzyl viologen
-
best electron donor
-
-
?
selenate + reduced methyl viologen
selenite + H2O + oxidized methyl viologen
-
-
-
-
?
selenate + reduced methyl viologen
selenite + H2O + oxidized methyl viologen
-
11% of the activity with benzyl viologen
-
-
?
additional information
?
-
-
NADH, succinate, and lactate are no electron donors
-
-
?
additional information
?
-
-
no activity with nitrate, nitrite, sulfate, and chlorate
-
-
?
additional information
?
-
-
no activity with nitrate, nitrite, sulfate, and chlorate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
selenate + electron donor
selenite + H2O + oxidized electron donor
selenate + H2
selenite + H2O
-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
selenate + electron donor
selenite + H2O + oxidized electron donor
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
-
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + electron donor
selenite + H2O + oxidized electron donor
selenate is the terminal electron acceptor in dissimilatory selenate reduction
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
-
-
-
-
?
selenate + reduced acceptor
selenite + H2O + acceptor
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
iron-sulfur centre
-
at least 2 [Fe-S]-centre as prosthetic groups per enzyme molecule
cytochrome b
-
-
-
cytochrome b
-
1 cytochrome b per alphabetagamma-trimer
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
selenium
-
isolated enzyme contains a reduced form of selenium, probably as selenocysteine
sulfur
-
iron-sulfur centre
Iron
-
part of at least 2 iron-sulfur centres per enzyme molecule and of the heme group of cytochrome b
Iron
-
12.9 mol per mol of enzyme, based on MW 159000
Iron
-
iron-sulfur centre
Iron
-
[3Fe4S]1+ and [4Fe4S]1+ centres
Molybdenum
-
-
Molybdenum
-
1 molybdenum per mol of trimer
Molybdenum
-
Mo-S, Mo=O and Mo-O bound to enzyme
Molybdenum
-
present at the active site
Molybdenum
-
type II molybdoenzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
tungstate
-
SER isolated from periplasmic fractions from cells grown on 1 mM tungstate display selenate reductase activities with a 20fold reduction in Vmax and a 23fold increase in substrate binding affinity. The thermo-stability and pH dependence of tungsten-SER is shown to be similar to that observed for molybdenum-SER
additional information
-
no inhibition by nitrate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
selenate
-
induction of enzyme activity when included in growth medium
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0007
selenate
-
tungsten-SER, pH and temperature not specified in the publication, Vmax: 0.01 micromol/min/mg
0.016
selenate
-
molybdenum-SER, pH and temperature not specified in the publication, Vmax: 0.2 micromol/min/mg
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
additional information
-
activity in nirate reductase deficient mutants under different growth conditions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
65
-
optimal temperature for molybdenum-SER
80
-
optimal temperature for tungsten-SER is higher than 80°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
UniProt
brenda
-
-
-
brenda
alpha, beta, and gamma subunits serA, serB, and serC of selenate reductase; from selenate-reducing membrane biofilm reactor (MBfR) biofilms
UniProt
brenda
selenate-respiring bacterium
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
-
-
brenda
-
loosely associated with the cytoplasmic membrane
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SERA_THASE
918
0
103407
Swiss-Prot
-
SERB_THASE
327
0
37122
Swiss-Prot
-
SERC_THASE
239
0
25564
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
37000
-
1 * 99000, alpha, + 1 * 37000, beta, + 1 * 23000, gamma, SDS-PAGE
99000
-
1 * 99000, alpha, + 1 * 37000, beta, + 1 * 23000, gamma, SDS-PAGE
180000
-
-
23000
-
1 * 99000, alpha, + 1 * 37000, beta, + 1 * 23000, gamma, SDS-PAGE
23000
-
1 * 96000, alpha, + 1 * 40000, beta, + 1 * 23000, gamma, SDS-PAGE
23000
-
alphabetagamma, 1 * 96000 + 1 * 40000 + 1 * 23000
23000
-
1 * 96000 + 1 * 40000 + 1 * 23000, SER consists of three subunits SerA (96 kDa), SerB (40 kDa), and SerC (23 kDa)
40000
-
1 * 96000, alpha, + 1 * 40000, beta, + 1 * 23000, gamma, SDS-PAGE
40000
-
alphabetagamma, 1 * 96000 + 1 * 40000 + 1 * 23000
40000
-
1 * 96000 + 1 * 40000 + 1 * 23000, SER consists of three subunits SerA (96 kDa), SerB (40 kDa), and SerC (23 kDa)
96000
-
1 * 96000, alpha, + 1 * 40000, beta, + 1 * 23000, gamma, SDS-PAGE
96000
-
alphabetagamma, 1 * 96000 + 1 * 40000 + 1 * 23000
96000
-
1 * 96000 + 1 * 40000 + 1 * 23000, SER consists of three subunits SerA (96 kDa), SerB (40 kDa), and SerC (23 kDa)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
trimer
-
1 * 99000, alpha, + 1 * 37000, beta, + 1 * 23000, gamma, SDS-PAGE
trimer
-
1 * 96000, alpha, + 1 * 40000, beta, + 1 * 23000, gamma, SDS-PAGE
trimer
-
alpha, beta, gamma
trimer
-
alphabetagamma, 1 * 96000 + 1 * 40000 + 1 * 23000
trimer
-
1 * 96000 + 1 * 40000 + 1 * 23000, SER consists of three subunits SerA (96 kDa), SerB (40 kDa), and SerC (23 kDa)
additional information
-
the gamma subunit may be identical with the cytochrome b
additional information
-
1 cytochrome b per alphabetagamma-complex
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
construction of Tn5 insertion mutants by transposon mutagenesis using Escherichia coli strain S17-1 as partner, loss of activity
additional information
-
construction of Tn5 insertion mutants by transposon mutagenesis using Escherichia coli strain S17-1 as partner, loss of activity
additional information
development of a serA gene-based PCR primer set to target selenate reductase (SerA) for detecting selenate reducing bacteria (SeRB) in biofilms, the primer set is specific for selenate reducing bacteria but not denitrifying bacteria, overview
additional information
-
development of a serA gene-based PCR primer set to target selenate reductase (SerA) for detecting selenate reducing bacteria (SeRB) in biofilms, the primer set is specific for selenate reducing bacteria but not denitrifying bacteria, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
57fold, to near homogeneity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DNA sequence determination and analysis, contruction of gene bank, genomic organisationand potential function of: genes serA, serB, and serC, additional overlapping serD
gene serA, DNA and amino acid sequence determination and analysis, phylogenetic analysis, quantitative PCR expression analysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Rech, S.A.; Macy, J.M.
The terminal reductases for selenate and nitrate respiration in Thauera selenatis are two distinct enzymes
J. Bacteriol.
174
7316-7320
1992
Thauera selenatis
brenda
Schroder, I.; Rech, S.; Krafft, T.; Macy, J.M.
Purification and characterization of the selenate reductase from Thauera selenatis
J. Biol. Chem.
272
23765-23768
1997
Thauera selenatis
brenda
Stolz, J.F.; Oremland, R.S.
Bacterial respiration of arsenic and selenium
FEMS Microbiol. Rev.
23
615-627
1999
Anaerobacillus arseniciselenatis, Sulfurospirillum barnesii, Sulfurospirillum barnesii SES-3, Thauera selenatis
brenda
Krafft, T.; Bowen, A.; Theis, F.; Macy, J.M.
Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase of Thauera selenatis
DNA Seq.
10
365-377
2000
Thauera selenatis (Q9S1H0 and Q9S1G9 and Q9S1G7), Thauera selenatis
brenda
Maher, M.J.; Macy, J.M.
Crystallization and preliminary X-ray analysis of the selenate reductase from Thauera selenatis
Acta Crystallogr. Sect. D
58
706-708
2002
Thauera selenatis
brenda
Watts, C.A.; Ridley, H.; Dridge, E.J.; Leaver, J.T.; Reilly, A.J.; Richardson, D.J.; Butler, C.S.
Microbial reduction of selenate and nitrate: common themes and variations
Biochem. Soc. Trans.
33
173-175
2005
Enterobacter cloacae, Enterobacter cloacae SLDa-1, Sulfurospirillum barnesii, Thauera selenatis
brenda
Maher, M.J.; Santini, J.; Pickering, I.J.; Prince, R.C.; Macy, J.M.; George, G.N.
X-ray absorption spectroscopy of selenate reductase
Inorg. Chem.
43
402-404
2004
Thauera selenatis
brenda
Dridge, E.J.; Watts, C.A.; Jepson, B.J.; Line, K.; Santini, J.M.; Richardson, D.J.; Butler, C.S.
Investigation of the redox centres of periplasmic selenate reductase from Thauera selenatis by EPR spectroscopy
Biochem. J.
408
19-28
2007
Thauera selenatis
brenda
Dridge, E.J.; Butler, C.S.
Thermostable properties of the periplasmic selenate reductase from Thauera selenatis
Biochimie
92
1268-1273
2010
Thauera selenatis
brenda
Lowe, E.C.; Bydder, S.; Hartshorne, R.S.; Tape, H.L.; Dridge, E.J.; Debieux, C.M.; Paszkiewicz, K.; Singleton, I.; Lewis, R.J.; Santini, J.M.; Richardson, D.J.; Butler, C.S.
Quinol-cytochrome c oxidoreductase and cytochrome c4 mediate electron transfer during selenate respiration in Thauera selenatis
J. Biol. Chem.
285
18433-18442
2010
Thauera selenatis
brenda
Wen, L.L.; Lai, C.Y.; Yang, Q.; Chen, J.X.; Zhang, Y.; Ontiveros-Valencia, A.; Zhao, H.P.
Quantitative detection of selenate-reducing bacteria by real-time PCR targeting the selenate reductase gene
Enzyme Microb. Technol.
85
19-24
2016
Pseudomonas stutzeri, Thauera selenatis (Q9S1H0 and Q9S1G9 and Q9S1G7), Thauera selenatis, Thauera selenatis ATCC 55363 (Q9S1H0 and Q9S1G9 and Q9S1G7), Thauera sp.
brenda
Transporter Classification Database (TCDB):
5.A.3.8.1