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Information on EC 1.97.1.9 - selenate reductase and Organism(s) Thauera selenatis and UniProt Accession Q9S1H0

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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.
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Thauera selenatis
UNIPROT: Q9S1H0 not found.
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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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
selenate reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
selenite + H2O + acceptor = selenate + reduced acceptor
show the reaction diagram
electron transport mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
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-
-
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reduction
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-
-
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PATHWAY SOURCE
PATHWAYS
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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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 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 + reduced acceptor
selenite + H2O + acceptor
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 + oxidized methyl viologen
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
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
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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
selenium
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isolated enzyme contains a reduced form of selenium, probably as selenocysteine
sulfur
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iron-sulfur centre
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tungstate
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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
-
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
0.0007 - 0.016
selenate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
387
selenate
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pH 6.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
purified enzyme
additional information
-
activity in nirate reductase deficient mutants under different growth conditions
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
optimal temperature for molybdenum-SER
80
-
optimal temperature for tungsten-SER is higher than 80°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SERA_THASE
918
0
103407
Swiss-Prot
-
SERB_THASE
327
0
37122
Swiss-Prot
-
SERC_THASE
239
0
25564
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
180000
23000
37000
-
1 * 99000, alpha, + 1 * 37000, beta, + 1 * 23000, gamma, SDS-PAGE
40000
96000
99000
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1 * 99000, alpha, + 1 * 37000, beta, + 1 * 23000, gamma, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
57fold, to near homogeneity
-
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
gene serA, DNA and amino acid sequence determination and analysis, phylogenetic analysis, quantitative PCR expression analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Dridge, E.J.; Butler, C.S.
Thermostable properties of the periplasmic selenate reductase from Thauera selenatis
Biochimie
92
1268-1273
2010
Thauera selenatis
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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.
Manually annotated by BRENDA team