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Literature summary for 2.7.9.3 extracted from

  • 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 (2015), Genome Res., 25, 1256-1267.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
a single SPS gene, phylogenetic analysis Ciona intestinalis
gene ptuf/SelD or SPS1, genetic structure analysis, SPS1-UGA might perhaps be translated by a readthrough mechanism not involving Sec insertion. In this respect, there is growing evidence for abundant stop codon readthrough in insects, with UGA being the most frequently observed readthrough codon in Drosophila Drosophila melanogaster
gene seld-1, genetic structure analysis Caenorhabditis elegans
gene SPS, phylogenetic analysis Oikopleura dioica
gene SPS, phylogenetic analysis Molgula tectiformis
gene SPS2, phylogenetic analysis Botryllus schlosseri

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli
Mg2+ required Homo sapiens
Mg2+ required Drosophila melanogaster
Mg2+ required Caenorhabditis elegans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + selenide + H2O Escherichia coli
-
AMP + selenophosphate + phosphate
-
?
ATP + selenide + H2O Homo sapiens
-
AMP + selenophosphate + phosphate
-
?
ATP + selenide + H2O Drosophila melanogaster
-
AMP + selenophosphate + phosphate
-
?
ATP + selenide + H2O Caenorhabditis elegans
-
AMP + selenophosphate + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Botryllus schlosseri
-
contains an active SPS2-Sec and an inactive SPS1-Gly isozyme
-
Caenorhabditis elegans O62461
-
-
Ciona intestinalis
-
-
-
Drosophila melanogaster O18373 gene ptuf/SelD or SPS1
-
Escherichia coli
-
-
-
Homo sapiens Q99611 Sephs2
-
Molgula tectiformis
-
contains an active SPS-Sec and an inactive SPS-Gly isozyme
-
no activity in Acyrthosiphon pisum
-
selenoprotein genes are converted to Cys homologues or lost, and the Sec machinery degenerated and/or disappeared
-
no activity in Coleoptera
-
selenoprotein genes are converted to Cys homologues or lost, and the Sec machinery degenerated and/or disappeared
-
no activity in Drosophila willistoni
-
-
-
no activity in Endopterygota
-
selenoprotein genes are converted to Cys homologues or lost, and the Sec machinery degenerated and/or disappeared
-
no activity in Hymenoptera
-
selenoprotein genes are converted to Cys homologues or lost, and the Sec machinery degenerated and/or disappeared
-
no activity in Lepidoptera
-
selenoprotein genes are converted to Cys homologues or lost, and the Sec machinery degenerated and/or disappeared
-
Oikopleura dioica
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + selenide + H2O
-
Escherichia coli AMP + selenophosphate + phosphate
-
?
ATP + selenide + H2O
-
Homo sapiens AMP + selenophosphate + phosphate
-
?
ATP + selenide + H2O
-
Drosophila melanogaster AMP + selenophosphate + phosphate
-
?
ATP + selenide + H2O
-
Caenorhabditis elegans AMP + selenophosphate + phosphate
-
?

Synonyms

Synonyms Comment Organism
SelD
-
Escherichia coli
SelD
-
Ciona intestinalis
SelD
-
Homo sapiens
SelD
-
Drosophila melanogaster
SelD
-
Oikopleura dioica
SelD
-
Molgula tectiformis
SelD
-
Botryllus schlosseri
seld-1
-
Caenorhabditis elegans
selenide water dikinase
-
Homo sapiens
selenide water dikinase
-
Drosophila melanogaster
selenide water dikinase
-
Caenorhabditis elegans
selenophosphate synthetase
-
Escherichia coli
selenophosphate synthetase
-
Ciona intestinalis
selenophosphate synthetase
-
Homo sapiens
selenophosphate synthetase
-
Drosophila melanogaster
selenophosphate synthetase
-
Caenorhabditis elegans
selenophosphate synthetase
-
Oikopleura dioica
selenophosphate synthetase
-
Molgula tectiformis
selenophosphate synthetase
-
Botryllus schlosseri
Sephs2
-
Homo sapiens
SPS
-
Escherichia coli
SPS
-
Ciona intestinalis
SPS
-
Caenorhabditis elegans
SPS
-
Oikopleura dioica
SPS
-
Molgula tectiformis
SPS
-
Botryllus schlosseri
SPS1
-
Drosophila melanogaster
Sps2
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
Escherichia coli
ATP
-
Homo sapiens
ATP
-
Drosophila melanogaster
ATP
-
Caenorhabditis elegans

General Information

General Information Comment Organism
evolution selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common, e.g. Drosophila melanogaster possesses three selenoprotein genes, while Drosophila willistoni has replaced Sec with Cys in them and lost the capacity to synthesize Sec. Unequal selective pressure on SPS1 and SPS2 genes after duplication, overview Drosophila melanogaster
evolution selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common. At the root of ascidians, the ancestral SPS2-Sec gene acquired a novel SPS-Gly transcript isoform through alternative exon usage at the 5'-end. Then, at the root of the ascidian lineage, Styelidae and Pyuridae, the SPS-Sec transcript of this dual SPS1/SPS2 gene (SPS-ae) retrotransposed to the genome creating a novel SPS2-Sec gene (GDR). This presumably triggered the loss of Sec from the parental gene, which, because both the SECIS and the UGA containing exon degenerated (SL), specialized only in the production of SPS1-Gly. Parallel gene duplications of SPS proteins in metazoa, phylogenetic analysis, overview Ciona intestinalis
evolution selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common. At the root of ascidians, the ancestral SPS2-Sec gene acquired a novel SPS-Gly transcript isoform through alternative exon usage at the 5'-end. Then, at the root of the ascidian lineage, Styelidae and Pyuridae, the SPS-Sec transcript of this dual SPS1/SPS2 gene (SPS-ae) retrotransposed to the genome creating a novel SPS2-Sec gene (GDR). This presumably triggered the loss of Sec from the parental gene, which, because both the SECIS and the UGA containing exon degenerated (SL), specialized only in the production of SPS1-Gly. Parallel gene duplications of SPS proteins in metazoa, phylogenetic analysis, overview Oikopleura dioica
evolution selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common. At the root of ascidians, the ancestral SPS2-Sec gene acquired a novel SPS-Gly transcript isoform through alternative exon usage at the 5'-end. Then, at the root of the ascidian lineage, Styelidae and Pyuridae, the SPS-Sec transcript of this dual SPS1/SPS2 gene (SPS-ae) retrotransposed to the genome creating a novel SPS2-Sec gene (GDR). This presumably triggered the loss of Sec from the parental gene, which, because both the SECIS and the UGA containing exon degenerated (SL), specialized only in the production of SPS1-Gly. Parallel gene duplications of SPS proteins in metazoa, phylogenetic analysis, overview Molgula tectiformis
evolution selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common. At the root of ascidians, the ancestral SPS2-Sec gene acquired a novel SPS-Gly transcript isoform through alternative exon usage at the 5'-end. Then, at the root of the ascidian lineage, Styelidae and Pyuridae, the SPS-Sec transcript of this dual SPS1/SPS2 gene (SPS-ae) retrotransposed to the genome creating a novel SPS2-Sec gene (GDR). This presumably triggered the loss of Sec from the parental gene, which, because both the SECIS and the UGA containing exon degenerated (SL), specialized only in the production of SPS1-Gly. Parallel gene duplications of SPS proteins in metazoa, phylogenetic analysis, overview Botryllus schlosseri
evolution selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common. In Caenorhabditis elegans, the entire pathway is maintained only to synthesize a single selenoprotein. Unequal selective pressure on SPS1 and SPS2 genes after duplication, overview Caenorhabditis elegans
evolution selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common. Phylogenetic profile of SPS and selenium utilization traits in prokaryotes, overview Escherichia coli
evolution selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common. Unequal selective pressure on SPS1 and SPS2 genes after duplication, overview Homo sapiens
additional information SPS2, i.e. Sephs2, invertebrates is a selenoprotein Homo sapiens
physiological function Drosophila SPS1 (i.e., ptuf/SelD) lacks the ability to catalyze selenide-dependent ATP hydrolysis or to complement SelD deficiency in Escherichia coli. Drosophila SPS1 has been proposed to be involved in vitamin B6 metabolism and in redox homeostasis since it protects from damage induced by reactive oxygen species Drosophila melanogaster