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Information on EC 2.7.9.3 - selenide, water dikinase and Organism(s) Homo sapiens and UniProt Accession P49903

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EC Tree
IUBMB Comments
Mg2+-dependent enzyme identified in Escherichia coli
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This record set is specific for:
Homo sapiens
UNIPROT: P49903
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
selenophosphate synthetase, sephs2, selenophosphate synthetase 2, selenophosphate synthetase 1, sps 1, dsps2, sps-1, seld protein, selenophosphate synthase, selenophosphate synthetase-1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
selenophosphate synthetase 1
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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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selenide water dikinase
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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 1
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selenophosphate synthetase 2
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synthetase, selenophosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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phospho group transfer
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
ATP:selenide, water phosphotransferase
Mg2+-dependent enzyme identified in Escherichia coli
CAS REGISTRY NUMBER
COMMENTARY hide
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) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + selenide + H2O
AMP + selenophosphate + phosphate
show the reaction diagram
ATP + selenide + H2O
AMP + selenophosphate + phosphate
show the reaction diagram
additional information
?
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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
ATP + selenide + H2O
AMP + selenophosphate + phosphate
show the reaction diagram
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-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
show the reaction diagram
additional information
?
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SPS2 is involved in the synthesis of selenophosphate for Sel synthesis, selen and selenoprotien metabolism, physiological functions, detailed overview
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8-azido-ATP
competitive to ATP
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026
ATP
pH 7.0, temperature not specified in the publication, recombinant His6-tagged enzyme mutant Sephs2-U60C
additional information
additional information
steady-state kinetics for the C-terminally His6-tagged enzyme mutant Sephs2-U60C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0058
ATP
pH 7.0, temperature not specified in the publication, recombinant His6-tagged enzyme mutant Sephs2-U60C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
SPS2 shows a broad tissue distribution
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
SEPHS2 is responsible for de novo synthesis of monoselenophosphate. SEPHS2 interacts with SEPSECS and SEPHS1
additional information
SPS2, i.e. Sephs2, invertebrates is a selenoprotein
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SPS1_HUMAN
392
0
42911
Swiss-Prot
other Location (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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oligomer
selenocysteine synthase (SEPSECS), SECp43, and selenophosphate synthetases SEPHS1 and SEPHS2 form oligomers in eukaryotic cells
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structures of selenophosphate synthetase 1 and of selenophosphate synthetase 1 complexed with AMPCP and K+ are solved to a resolution of 2.0 and 1.9 A, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G269C
site-directed mutagenesis, reduced activity, slightly reduced ATP binding
G271R
site-directed mutagenesis, reduced activity, slightly reduced ATP binding
G274A
site-directed mutagenesis, reduced activity and ATP binding
G274D
site-directed mutagenesis, reduced activity, no ATP binding
G274V
site-directed mutagenesis, no activity and ATP binding
H275N
site-directed mutagenesis, reduced activity, no ATP binding
H275Y
site-directed mutagenesis, increased catalytic activity and ATP binding
Sec60C
site-directed mutagenesis, the in-frame opal codon for Sec60 is altered to Cys-coding TGT in mutant Sephs2U60C, the substitution of active site Sec with Cys does not significantly perturb the catalytic function of the His6-tagged human Sephs2
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
on a Ni-chelating column, the His-tag is removed by thrombin digestion, further purification by gel-filtration
recombinant C-terminally His6-tagged enzyme mutant Sephs2U60C from Escherichia coli Rosetta (DE3) pLysS by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene selD, DNA sequence determination and analysis, subcloning and transient expression in enzyme deficient Escherichia coli resulting in poor complemetation of the bacteria by the human gene, and expression in mammalian HtTA cells together with human type I iodothyronine 5'-deiodinase and Xenopus tRNASeC
into the vector pET28a for expression in Escherichia coli Rosetta DE3 cells
DNA sequence determination and analysis
gene Sephs2, recombinant expression of C-terminally His6-tagged enzyme mutant Sephs2U60C in Escherichia coli Rosetta (DE3) pLysS
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the levels of the major type and DELTAE8 splice variants of selenophosphate synthetase 1 are gradually increased until G2/M phase and then gradually decreases. Splice variant DELTAE2 expression peaks at mid-S phase and then gradually decreases
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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Sps1 and its reaction product selenophosphate might play a role in cancer prevention and therapy when a modulation of the enzyme activity is combined with cancer therapies
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Low, S.C.; Harney, J.W.; Berry, M.J.
Cloning and functional characterization of human selenophosphate synthetase, an essential component of selenoprotein synthesis
J. Biol. Chem.
270
21659-21664
1995
Homo sapiens (P49903), Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Tamura, T.; Yamamoto, S.; Takahata, M.; Sakaguchi, H.; Tanaka, H.; Stadtman, T.C.; Inagaki, K.
Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling L-selenocysteine and Sps2 for selenite assimilation
Proc. Natl. Acad. Sci. USA
101
16162-16167
2004
Homo sapiens
Manually annotated by BRENDA team
Chung, H.J.; Yoon, S.I.; Shin, S.H.; Koh, Y.A.; Lee, S.J.; Lee, Y.S.; Bae, S.
p53-mediated enhancement of radiosensitivity by selenophosphate synthetase 1 overexpression
J. Cell. Physiol.
209
131-141
2006
Homo sapiens
Manually annotated by BRENDA team
Pappas, A.C.; Zoidis, E.; Surai, P.F.; Zervas, G.
Selenoproteins and maternal nutrition
Comp. Biochem. Physiol. B
151
361-372
2008
Homo sapiens (Q99611)
Manually annotated by BRENDA team
Wang, K.T.; Wang, J.; Li, L.F.; Su, X.D.
Crystal structures of catalytic intermediates of human selenophosphate synthetase 1
J. Mol. Biol.
390
747-759
2009
Homo sapiens (P49903), Homo sapiens
Manually annotated by BRENDA team
Kim, J.Y.; Lee, K.H.; Shim, M.S.; Shin, H.; Xu, X.M.; Carlson, B.A.; Hatfield, D.L.; Lee, B.J.
Human selenophosphate synthetase 1 has five splice variants with unique interactions, subcellular localizations and expression patterns
Biochem. Biophys. Res. Commun.
397
53-58
2010
Homo sapiens
Manually annotated by BRENDA team
Kamada, S.; Okugochi, T.; Asano, K.; Tobe, R.; Mihara, H.; Nemoto, M.; Inagaki, K.; Tamura, T.
A non-radioactive assay for selenophosphate synthetase activity using recombinant pyruvate pyrophosphate dikinase from Thermus thermophilus HB8
Biosci. Biotechnol. Biochem.
80
1970-1972
2016
Homo sapiens (Q99611)
Manually annotated by BRENDA team
Mariotti, M.; Santesmasses, D.; Capella-Gutierrez, S.; Mateo, A.; Arnan, C.; Johnson, R.; D'Aniello, S.; Yim, S.H.; Gladyshev, V.N.; Serras, F.; Corominas, M.; Gabaldon, T.; Guigo, R.
Evolution of selenophosphate synthetases: emergence and relocation of function through independent duplications and recurrent subfunctionalization
Genome Res.
25
1256-1267
2015
Ciona intestinalis, Escherichia coli, no activity in Hymenoptera, Oikopleura dioica, Molgula tectiformis, Botryllus schlosseri, no activity in Lepidoptera, no activity in Coleoptera, no activity in Endopterygota, no activity in Acyrthosiphon pisum, no activity in Drosophila willistoni, Drosophila melanogaster (O18373), Caenorhabditis elegans (O62461), Homo sapiens (Q99611)
Manually annotated by BRENDA team
Oudouhou, F.; Casu, B.; Dopgwa Puemi, A.S.; Sygusch, J.; Baron, C.
Analysis of Novel interactions between components of the selenocysteine biosynthesis pathway, SEPHS1, SEPHS2, SEPSECS, and SECp43
Biochemistry
56
2261-2270
2017
Homo sapiens (Q99611)
Manually annotated by BRENDA team
Na, J.; Jung, J.; Bang, J.; Lu, Q.; Carlson, B.A.; Guo, X.; Gladyshev, V.N.; Kim, J.; Hatfield, D.L.; Lee, B.J.
Selenophosphate synthetase 1 and its role in redox homeostasis, defense and proliferation
Free Radic. Biol. Med.
127
190-197
2018
Escherichia coli, Homo sapiens (Q99611), Homo sapiens
Manually annotated by BRENDA team