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Information on EC 2.7.9.3 - selenide, water dikinase and Organism(s) Clostridioides difficile and UniProt Accession Q182I1

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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:
Clostridioides difficile
UNIPROT: Q182I1
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Word Map
The taxonomic range for the selected organisms is: Clostridioides difficile
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 synthetase-1, selenophosphate synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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
synthetase, selenophosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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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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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene selD
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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the selD CRISPR deletion mutant has a growth defect in protein-rich medium and mimicks the phenotype of a generated TargeTron selD mutation
physiological function
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the enzyme is essential for the specific incorporation of selenium into selenoproteins
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene selD, DNA and amino acid sequence determination and analysis, phylogenetic profiling
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Haft, D.H.; Self, W.T.
Orphan SelD proteins and selenium-dependent molybdenum hydroxylases
Biol. Direct
3
4
2008
Escherichia coli, Enterococcus faecalis, Clostridioides difficile (Q182I1), Haloarcula marismortui (Q5V6B2), Haloarcula marismortui
Manually annotated by BRENDA team
McAllister, K.N.; Bouillaut, L.; Kahn, J.N.; Self, W.T.; Sorg, J.A.
Using CRISPR-Cas9-mediated genome editing to generate C. difficile mutants defective in selenoproteins synthesis
Sci. Rep.
7
14672
2017
Clostridioides difficile, Clostridioides difficile R20291
Manually annotated by BRENDA team