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Information on EC 2.9.1.2 - O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA synthase and Organism(s) Methanococcus maripaludis and UniProt Accession Q6LZM9

for references in articles please use BRENDA:EC2.9.1.2
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IUBMB Comments
A pyridoxal-phosphate protein . In archaea and eukarya selenocysteine formation is achieved by a two-step process: EC 2.7.1.164 (O-phosphoseryl-tRNASec kinase) phosphorylates the endogenous L-seryl-tRNASec to O-phospho-L-seryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by Sep-tRNA:Sec-tRNA synthase.
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Methanococcus maripaludis
UNIPROT: Q6LZM9
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Word Map
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  • 2.9.1.2
  • selenoproteins
  • autoantibodies
  • sec-trnasec
  • ama-m2
  • cerebello-cerebral
  • sep-trna:sec-trna
  • trna-dependent
  • anti-soluble
  • trnasersec
  • secisbp2
  • selenoproteome
  • efsec
  • anti-smooth
  • anti-liver
  • selenoenzymes
  • sephs2
The taxonomic range for the selected organisms is: Methanococcus maripaludis
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
sepsecs, sla/lp, o-phosphoseryl-trna:selenocysteinyl-trna synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
O-phosphoseryl-tRNA:selenocysteinyl-tRNA synthase
-
SYSTEMATIC NAME
IUBMB Comments
selenophosphate:O-phospho-L-seryl-tRNASec selenium transferase
A pyridoxal-phosphate protein [4]. In archaea and eukarya selenocysteine formation is achieved by a two-step process: EC 2.7.1.164 (O-phosphoseryl-tRNASec kinase) phosphorylates the endogenous L-seryl-tRNASec to O-phospho-L-seryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by Sep-tRNA:Sec-tRNA synthase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
O-phospho-L-seryl-tRNASec + selenophosphate
L-selenocysteinyl-tRNASec + phosphate
show the reaction diagram
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
O-phospho-L-seryl-tRNASec + selenophosphate
L-selenocysteinyl-tRNASec + phosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
Methanococcus maripaludis Mm900 is facultatively selenium-dependent with a single pathway of Sec-tRNASec formation. Seelenocysteine formation is abolished upon individually deleting the genes encoding selenophosphate synthetase, phosphoseryl-tRNASec kinase, or SepSecS. The resulting mutant strains can no longer grow on formate while growth with H2 + CO2 remains unaffected. Deletion of the phosphoseryl-tRNASec kinase and SepSecS genes is not possible unless the selenium-free [NiFe]-hydrogenases Frc and Vhc are expressed
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
a member of the Fold Type I pyridoxal 5'-phosphate enzyme family, forms an (alpha2)2 homotetramer through its N-terminal extension. The active site lies on the dimer interface with each monomer contributing essential residues
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapor diffusion method at 20°C, crystal structure of the enzyme complexed with pyridoxal 5'-phosphate at 2.5 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H166A
the mutant is partially active in forming Sec-tRNASec in vivo. In vitro, the mutant is partially active in forming Cys-tRNASec
H166F
mutant is inactive in vivo
H166Q
mutant is inactive in vivo
R307A
the mutant is significantly less active in L-selenocysteinyl-tRNASec formation in vivo and Cys-tRNASec formation in vitro
R72A
the mutant enzyme is significantly less active in L-selenocysteinyl-tRNASec formation in vivo and Cys-tRNASec formation in vitro. The mutant enzyme is unable to form L-selenocysteinyl-tRNASec in vitro
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Araiso, Y.; Palioura, S.; Ishitani, R.; Sherrer, R.L.; O'Donoghue, P.; Yuan, J.; Oshikane, H.; Domae, N.; Defranco, J.; Sll, D.; Nureki, O.
Structural insights into RNA-dependent eukaryal and archaeal selenocysteine formation
Nucleic Acids Res.
36
1187-1199
2008
Methanococcus maripaludis (Q6LZM9), Methanococcus maripaludis
Manually annotated by BRENDA team
Yuan, J.; Palioura, S.; Salazar, J.C.; Su, D.; O'Donoghue, P.; Hohn, M.J.; Cardoso, A.M.; Whitman, W.B.; Sll, D.
RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea
Proc. Natl. Acad. Sci. USA
103
18923-18927
2006
Methanocaldococcus jannaschii (Q58027), Methanococcus maripaludis (Q6LZM9), Homo sapiens (Q9HD40), Homo sapiens
Manually annotated by BRENDA team
Hohn, M.J.; Palioura, S.; Su, D.; Yuan, J.; Soell, D.
Genetic analysis of selenocysteine biosynthesis in the archaeon Methanococcus maripaludis
Mol. Microbiol.
81
249-258
2011
Methanococcus maripaludis (Q6LZM9), Methanococcus maripaludis
Manually annotated by BRENDA team