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Information on EC 2.7.9.3 - selenide, water dikinase and Organism(s) Mus musculus and UniProt Accession Q8BH69
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2.7.9.3 selenide, water dikinaseIUBMB Comments
Mg2+-dependent enzyme identified in Escherichia coli
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Word Map
- 2.7.9.3
-
selenoproteins
- monoselenophosphate
-
deiodinases
-
iodothyronine
-
selenocysteine-containing
- trnasec
-
secis
-
2-selenouridine
-
selenoproteome
- seryl-trna
- sepsecs
-
stadtman
-
5-methylaminomethyl-2-selenouridine
- seryl-trnasec
-
selenoenzymes
- txnrd3
-
selenium-dependent
-
trnasersec
- l-selenocysteine
- medicine
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
selenophosphate synthetase, sephs2, selenophosphate synthetase 2, selenophosphate synthetase 1, dsps2, sps 1, sps-1, seld protein, selenophosphate synthase, selenophosphate synthetase-1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GenBank AE000719-derived protein GI 2983519
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gene selD proteins
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kinase (phosphorylating), pyruvate-water di-
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Patufet protein
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proteins , gene selD (specific proteins and subclasses)
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proteins, gene selD
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pyruvate-water di-kinase (phosphorylating)
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SELD protein
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selenium donor protein
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selenophosphate synthase
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selenophosphate synthase (Aquifex aeolicus gene selD)
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selenophosphate synthetase
selenophosphate synthetase 2
Sps2
synthetase, selenophosphate
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selenophosphate synthetase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
ATP:selenide, water phosphotransferase
Mg2+-dependent enzyme identified in Escherichia coli
CAS REGISTRY NUMBER
COMMENTARY
151125-25-6
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204795-23-3
selenophosphate synthase (Aquifex aeolicus gene selD), genBank AE000719-derived protein GI 2983519
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + selenide
AMP + selenophosphate + phosphate
SPS2 acts as an autoregulator of selenoprotein synthesis, selenocysteine biosynthesis, overview
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-
?
ATP + selenide
AMP + selenophosphate + phosphate
SPS2, the catalytically important selenocysteine residue is located at position 63
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?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
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specific for ATP
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?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
required for synthesis of selenocysteine and seleno-tRNAs
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?
additional information
?
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SPS1 probably has a specialized, non-essential role in selenoprotein metabolism
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?
additional information
?
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SPS1 probably has a specialized, non-essential role in selenoprotein metabolism
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?
additional information
?
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SPS1 probably has a specialized, non-essential role in selenoprotein metabolism
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?
additional information
?
-
Sps2 is both a selenoprotein and a factor involved in synthesis of other selenoproteins
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?
additional information
?
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Sps2 is both a selenoprotein and a factor involved in synthesis of other selenoproteins
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?
additional information
?
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SPS2 is essential for generating the selenium donor for selenocysteine biosynthesis in mammals
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?
additional information
?
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SPS2 is essential for generating the selenium donor for selenocysteine biosynthesis in mammals
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?
additional information
?
-
SPS2 is essential for generating the selenium donor for selenocysteine biosynthesis in mammals
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?
additional information
?
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no activity by selenophosphate synthetase 1
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?
additional information
?
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Se in the form of the amino acid, selenocysteine, is incorporated into selenoproteins at UGA codons
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?
additional information
?
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Se in the form of the amino acid, selenocysteine, is incorporated into selenoproteins at UGA codons
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + selenide + H2O
AMP + selenophosphate + phosphate
required for synthesis of selenocysteine and seleno-tRNAs
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
SPS2 acts as an autoregulator of selenoprotein synthesis, selenocysteine biosynthesis, overview
-
-
?
additional information
?
-
-
SPS1 probably has a specialized, non-essential role in selenoprotein metabolism
-
-
?
additional information
?
-
SPS1 probably has a specialized, non-essential role in selenoprotein metabolism
-
-
?
additional information
?
-
SPS1 probably has a specialized, non-essential role in selenoprotein metabolism
-
-
?
additional information
?
-
Sps2 is both a selenoprotein and a factor involved in synthesis of other selenoproteins
-
-
?
additional information
?
-
-
Sps2 is both a selenoprotein and a factor involved in synthesis of other selenoproteins
-
-
?
additional information
?
-
-
SPS2 is essential for generating the selenium donor for selenocysteine biosynthesis in mammals
-
-
?
additional information
?
-
SPS2 is essential for generating the selenium donor for selenocysteine biosynthesis in mammals
-
-
?
additional information
?
-
SPS2 is essential for generating the selenium donor for selenocysteine biosynthesis in mammals
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
-
the optimal range for the molar ratio of Mg2+ to ATP is between 2:1 and 4:1
Mg2+
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mouse SPS2-CYS expressed in Escherichia coli requires Mg2+, a molar ratio of Mg2+ to ATP in the range 2:1 or 4:1 is optimal
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Na+
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5-20 mM Na+ has little effect on enzyme activity in the presence or absence of 1.5 mM K+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
tissue distribution and content of selenoproteins, overview
additional information
-
tissue distribution and content of selenoproteins, overview
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
systemic SPS1 deficiency in Sps1 knockout mice leads to embryos are clearly underdeveloped by E8.5 and virtually resorbed by E14.5. The knockout of Sps1 in the liver preserves viability, but significantly affects the expression of a large number of mRNAs involved in cancer, embryonic development, and the glutathione system, especially extreme deficiency of glutaredoxin 1 (GLRX1) and glutathione-S-transferase omega 1. Targeted removal of SPS1 in F9 cells, a mouse embryonal carcinoma cell line, affects the glutathione system proteins and accordingly leads to the accumulation of hydrogen peroxide in the cell. Hydrogen peroxide accumulates due to the downregulation of GLRX1 in SPS1-deficient F9 cells. Overexpression of mouse or human GLRX1 leads to a reversal of observed increases in reactive oxygen species in the F9 SPS1/GLRX1-deficient cells and result in levels that are similar to those in F9 SPS1-sufficient cells. Loss of Sps1 in the liver affects iron and manganese levels. The expression of genes encoding proteins responsible for the de novo synthesis of glutathione, such as glutamate cysteine ligase catalytic subunit (GCLC), glutamate-cysteine modifier subunit (GCLM), and glutathione synthetase (GSS), is not affected by a deficiency in SPS1
physiological function
isozyme SPS1 is an essential mammalian enzyme with roles in regulating redox homeostasis and controlling cell growth. Isozyme SPS1 plays a role in supporting and/or sustaining cancer
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SPS1_MOUSE
392
0
42907
Swiss-Prot
other Location (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Sec63C
site-directed mutagenesis, SPS2 mutant Sec63Cys catalyzes the selenide-dependent synthesis of selenophosphate
T29C
site-directed mutagenesis, the Thr29Cys mutant of SPS1 exhibits SPS activity
additional information
additional information
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knockdown of SPS1 has no effect. Transfection of SPS1 into SPS2-knockdown cells cannot restore selenoprotein biosynthesis/SPS2 function
additional information
knockdown of SPS1 has no effect. Transfection of SPS1 into SPS2-knockdown cells cannot restore selenoprotein biosynthesis/SPS2 function
additional information
knockdown of SPS1 has no effect. Transfection of SPS1 into SPS2-knockdown cells cannot restore selenoprotein biosynthesis/SPS2 function
additional information
generation of a Sps1 knockout mouse with systemic isozyme SPS1 deficiency via C57BL/6 x 129/SvJae embryonic stem cell electroporation. Embryonic lethality of the Sps1-/- mice. Targeted removal of SPS1 in F9 cells, a mouse embryonal carcinoma cell line, phenotype, overview. Construction of a knockdown-resistant (rescue) SPS1 expression vector via three silent point mutations that are introduced into the shRNA target sequence by two-step PCR
additional information
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generation of a Sps1 knockout mouse with systemic isozyme SPS1 deficiency via C57BL/6 x 129/SvJae embryonic stem cell electroporation. Embryonic lethality of the Sps1-/- mice. Targeted removal of SPS1 in F9 cells, a mouse embryonal carcinoma cell line, phenotype, overview. Construction of a knockdown-resistant (rescue) SPS1 expression vector via three silent point mutations that are introduced into the shRNA target sequence by two-step PCR
additional information
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knockdown of SPS2 in NIH3T3 cells using small interfering RNA results in severely impaired selenoprotein biosynthesis. Transfection of SPS2 into SPS2-knockdown cells restores selenoprotein biosynthesis, but expression of SPS1 cannot complement SPS2 function
additional information
knockdown of SPS2 in NIH3T3 cells using small interfering RNA results in severely impaired selenoprotein biosynthesis. Transfection of SPS2 into SPS2-knockdown cells restores selenoprotein biosynthesis, but expression of SPS1 cannot complement SPS2 function
additional information
knockdown of SPS2 in NIH3T3 cells using small interfering RNA results in severely impaired selenoprotein biosynthesis. Transfection of SPS2 into SPS2-knockdown cells restores selenoprotein biosynthesis, but expression of SPS1 cannot complement SPS2 function
additional information
mutation of the Sec moiety in SPS2 to Cys results in low enzyme activity of the mutant compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged SPS1 and His-tagged SPS2 mutant Sec69Cys from Escherichia coli strain Rosetta (DE3) to homogeneity by affinity chromatography on a His-binding resin
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis of SPS2, complementation of SPS2 knockout NIH3T3 cells by expression of SPS2
DNA sequence determination and analysis, chromosomal mapping, expression in COS-7 cells as FLAG tagged enzyme
expression in Spodoptera frugiperda Sf9 insect cells via baculovirus infection, expression as N-FLAG tagged protein
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expression of His-tagged SPS1 and of His-tagged SPS2 mutant Sec69Cys in Escherichia coli strain Rosetta (DE3)
gene sps2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, sequence comparison, expression in Escherichia coli strain BL21(DE3)
NIH3T3 cells are stably transfected with the Tet-on U6 control construct or the Tet-siSPS2 construct and grown in the presence or absence of doxycycline for 3 d to induce SPS2 knockdown, then transiently transfected with pTriEX expression vector or the expression vector encoding SPS2 wild-type gene or SPS2 knock-in gene, SPS2 overexpression and functional restoration
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the mutated sps2 gene, which contains cysteine in the place of the TGA encoded selenocysteine in the wild-type, is expressed in Escherichia coli selD deficient mutant, MB08. Like the Escherichia coli wild-type selD gene, the mutant spos2 gene complements the selD mutation. Replacement of Cys with either Ala, Ser, or Thr results in a loss of ability to complement the selD mutation
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, I.Y.; Guimaraes, M.J.; Zlotnik, A.; Bazan, J.F.; Stadtman, T.C.
Fetal mouse selenophosphate synthetase 2 (SPS2): Characterization of the cysteine mutant form overproduced in a baculovirus-insect cell system
Proc. Natl. Acad. Sci. USA
94
418-421
1997
Mus musculus
Guimaraes, M.J.; Peterson, D.; Vicari, A.; Cocks, B.G.; Copeland, N.G.; Gilbert, D.J.; Jenkins, N.A.; Ferrick, D.A.; Kastelein, R.A.; Bazan, J.F.; Zlotnik, A.
Identification of a novel selD homolog from eukaryotes, bacteria, and archaea: Is there an autoregulatory mechanism in selenocysteine metabolism?
Proc. Natl. Acad. Sci. USA
93
15086-15091
1996
Haemophilus influenzae, Homo sapiens (Q99611), Homo sapiens, Methanocaldococcus jannaschii, Mus musculus (P97364), Mus musculus
Kim, T.S.; Yu, M.H.; Chung, Y.W.; Kim, J.; Choi, E.J.; Ahn, K.; Kim, I.Y.
Fetal mouse selenophosphate synthetase 2 (SPS2): biological activities of mutant forms in Escherichia coli
Mol. Cells
9
422-428
1999
Mus musculus
Xu, X.M.; Carlson, B.A.; Irons, R.; Mix, H.; Zhong, N.; Gladyshev, V.N.; Hatfield, D.L.
Selenophosphate synthetase 2 is essential for selenoprotein biosynthesis
Biochem. J.
404
115-120
2007
Mus musculus, Mus musculus (P97364), Mus musculus (Q8BH69)
Xu, X.M.; Carlson, B.A.; Zhang, Y.; Mix, H.; Kryukov, G.V.; Glass, R.S.; Berry, M.J.; Gladyshev, V.N.; Hatfield, D.L.
New developments in selenium biochemistry: selenocysteine biosynthesis in eukaryotes and archaea
Biol. Trace Elem. Res.
119
234-241
2007
Mus musculus (P97364)
Abe, K.; Mihara, H.; Nishijima, Y.; Kurokawa, S.; Esaki, N.
Functional analysis of two homologous mouse selenophosphate synthetases
Biomed. Res. Trace Elem.
19
76-79
2008
Mus musculus (P97364)
-
Hoffmann, P.R.; Hoege, S.C.; Li, P.A.; Hoffmann, F.W.; Hashimoto, A.C.; Berry, M.J.
The selenoproteome exhibits widely varying, tissue-specific dependence on selenoprotein P for selenium supply
Nucleic Acids Res.
35
3963-3973
2007
Mus musculus (P97364), Mus musculus
Xu, X.; Carlson, B.A.; Mix, H.; Zhang, Y.; Saira, K.; Glass, R.S.; Berry, M.J.; Gladyshev, V.N.; Hatfield, D.L.
Biosynthesis of selenocysteine on its tRNA in eukaryotes
PLoS Biol.
5
96-105
2007
Caenorhabditis elegans, Escherichia coli, Mus musculus (P97364), Drosophila melanogaster (Q9VKY8)
-
Yoo, M.H.; Xu, X.M.; Turanov, A.A.; Carlson, B.A.; Gladyshev, V.N.; Hatfield, D.L.
A new strategy for assessing selenoprotein function: siRNA knockdown/knock-in targeting the 3'-UTR
RNA
13
921-929
2007
Mus musculus
Tobe, R.; Carlson, B.A.; Huh, J.H.; Castro, N.P.; Xu, X.M.; Tsuji, P.A.; Lee, S.G.; Bang, J.; Na, J.W.; Kong, Y.Y.; Beaglehole, D.; Southon, E.; Seifried, H.; Tessarollo, L.; Salomon, D.S.; Schweizer, U.; Gladyshev, V.N.; Hatfield, D.L.; Lee, B.J.
Selenophosphate synthetase 1 is an essential protein with roles in regulation of redox homoeostasis in mammals
Biochem. J.
473
2141-2154
2016
Mus musculus (Q8BH69), Mus musculus, Mus musculus C57BL/6 (Q8BH69)
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