2.5.1.73: O-phospho-L-seryl-tRNA:Cys-tRNA synthase
This is an abbreviated version!
For detailed information about O-phospho-L-seryl-tRNA:Cys-tRNA synthase, go to the full flat file.
Word Map on EC 2.5.1.73
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2.5.1.73
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cys-trnacys
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methanogen
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archaea
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o-phosphoseryl-trna
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seprs
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cysteinyl-trna
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o-phosphoserine
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sulfur
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cysrs
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trna-dependent
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cysteinyl-trnacys
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jannaschii
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methanocaldococcus
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selenocysteine
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pyridoxal
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methanosarcina
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sec
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aminoacylation
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misacylated
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acetivorans
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auxotrophy
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persulfide
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relay
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sep-trna:sec-trna
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homocysteine
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fulgidus
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isoacceptors
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aminoacyl-trnas
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archaeoglobus
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trna-bound
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maripaludis
- 2.5.1.73
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cys-trnacys
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methanogen
- archaea
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o-phosphoseryl-trna
- seprs
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cysteinyl-trna
- o-phosphoserine
- sulfur
- cysrs
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trna-dependent
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cysteinyl-trnacys
- jannaschii
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methanocaldococcus
- selenocysteine
- pyridoxal
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methanosarcina
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sec
- aminoacylation
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misacylated
- acetivorans
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auxotrophy
- persulfide
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relay
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sep-trna:sec-trna
- homocysteine
- fulgidus
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isoacceptors
- aminoacyl-trnas
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archaeoglobus
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trna-bound
- maripaludis
Reaction
Synonyms
MJ1678, Sep-tRNA-Cys-tRNA synthase, Sep-tRNA:Cys-tRNA synthase, SepCysS
ECTree
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Substrates Products
Substrates Products on EC 2.5.1.73 - O-phospho-L-seryl-tRNA:Cys-tRNA synthase
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REACTION DIAGRAM
O-phospho-L-seryl-tRNASec + sulfide
L-cysteinyl-tRNASec + phosphate
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selenocysteinyl-specific O-phospho-L-seryl-tRNASec is recognized as a substrate, presence of the O-phospho-L-seryl moiety is crucial for recognition
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L-cysteinyl-tRNACys + phosphate
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O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
evolutionary history of Cys-tRNACys formation, overview
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O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
the in vivo sulfur donor is not determined
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O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
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O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
evolutionary history of Cys-tRNACys formation, overview
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O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
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O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
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evolutionary history of Cys-tRNACys formation, overview
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O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
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O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
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evolutionary history of Cys-tRNACys formation, overview
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L-cysteinyl-tRNACys + phosphate
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
modeling of tRNA binding, overview, sulfide, persulfide, and thiosulfate, but not cysteine, can function as sulfur donor in vitro, the active site is located deep within the large, basic cleft to accommodate Sep-tRNACys, binding modeling of Sep-tRNACys, overview, possibly the side-chain of a Cys residue in SepCysS becomes persulfided as a sulfur transfer intermediate state
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
the sulfur donor for this enzyme is unknown though in vitro sulfide is sufficient
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
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the natural sulfur donor is not characterized, the activity of SepCysS provides a means by which both cysteine and selenocysteine can be added to the genetic code, the enzyme is responsible for Cys-tRNACys synthesis together with the O-phosphoseryl-tRNA synthetase in the organism lacking the cysteinyl-tRNACys synthase, EC 6.1.1.16, overview
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
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sulfide e.g. from Na2S, anaerobic reaction
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
Methanocaldococcus jannaschii synthesizes Cys-tRNACys by an indirect pathway, whereby O-phosphoseryltRNA synthetase (SepRS) acylates tRNACys with phosphoserine (Sep), and Sep-tRNACys-tRNA synthase (SepCysS) converts the tRNA-bound phosphoserine to cysteine
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
Methanocaldococcus jannaschii synthesizes Cys-tRNACys by an indirect pathway, whereby O-phosphoseryltRNA synthetase (SepRS) acylates tRNACys with phosphoserine (Sep), and Sep-tRNACys-tRNA synthase (SepCysS) converts the tRNA-bound phosphoserine to cysteine. O-PhosphoseryltRNA synthetase and Sep-tRNACys-tRNA synthase bind the reaction intermediate O-phospho-L-serine-tRNACys tightly, and these two enzymes form a stable binary complex that promotes conversion of the intermediate to the product and sequesters the intermediate from binding to elongation factor EF-1a or infiltrating into the ribosome
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
all three highly conserved Cys residues in the enzyme (Cys64, Cys67, and Cys272) are essential for the sulfhydrylation reaction in vivo. Cys64 and Cys67 form a disulfide linkage and carry a sulfane sulfur in a portion of the enzyme. A persulfide group (containing a sulfane sulfur) is the proximal sulfur donor for cysteine biosynthesis
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
all three highly conserved Cys residues in the enzyme (Cys64, Cys67, and Cys272) are essential for the sulfhydrylation reaction in vivo. Cys64 and Cys67 form a disulfide linkage and carry a sulfane sulfur in a portion of the enzyme. A persulfide group (containing a sulfane sulfur) is the proximal sulfur donor for cysteine biosynthesis
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
the natural sulfur donor is not characterized, the activity of SepCysS provides a means by which both cysteine and selenocysteine can be added to the genetic code, the enzyme is responsible for Cys-tRNACys synthesis together with the O-phosphoseryl-tRNA synthetase in the organism containing a dispensable cysteinyl-tRNACys synthase, EC 6.1.1.16, overview
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
sulfide e.g. from Na2S, anaerobic reaction
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
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the sulfur donor for this enzyme is unknown though in vitro sulfide is sufficient. Methanococcus maripaludis encodes both the direct and indirect paths for Cys-tRNACys synthesis. While sepS (encoding SepRS) can be deleted when the organism is grown in the presence of Cys, pscS (encoding SepCysS) cannot. SepCysS may possess an additional function in Methanococcus maripaludis that is essential
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
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the sulfur donor for this enzyme is unknown though in vitro sulfide is sufficient
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
under steady-state conditions at 1-50 nM Sep-CysS, there is no reaction when O-phospho-L-seryl-tRNACys substrate levels are maintained below 0.01 mM, however, product formation is detected at 0.05 mM O-phospho-L-seryl-tRNACys
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
SepCysS exhibits substrate preference among the three Methanosarcina mazei tRNACys isoacceptors
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two-step Cys-tRNACys formation: in organisms like Archaeoglobus fulgidus lacking a canonical cysteinyl-tRNA synthetase for the direct Cys-tRNACys formation, Cys-tRNACys is produced by the indirect pathway, in which the non-canonical O-phosphoseryl-tRNA synthetase, SepRS, ligates the non-canonical amino acid O-phosphoserine, Sep, to tRNACys, and the Sep-tRNA:Cys-tRNA synthase converts the produced Sep-tRNACys to Cys-tRNACys, overview, the SepRS/SepCysS pathway is the sole route for cysteine biosynthesis in the organism
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additional information
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two-step Cys-tRNACys formation: in organisms like Archaeoglobus fulgidus lacking a canonical cysteinyl-tRNA synthetase for the direct Cys-tRNACys formation, Cys-tRNACys is produced by the indirect pathway, in which the non-canonical O-phosphoseryl-tRNA synthetase, SepRS, ligates the non-canonical amino acid O-phosphoserine, Sep, to tRNACys, and the Sep-tRNA:Cys-tRNA synthase converts the produced Sep-tRNACys to Cys-tRNACys, overview, the SepRS/SepCysS pathway is the sole route for cysteine biosynthesis in the organism
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additional information
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the active site contains an internal aldimine Lys209-PLP and the sulfate ion, SepCysS should not bind Sep-tRNASec and discriminate tRNACys from tRNASec on the basis of the differences in the length of the T-arms, or SepCysS recognizes the discriminator sequence, which is Ura73 in tRNACys and Gua73 in tRNASec, overview
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additional information
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the active site contains an internal aldimine Lys209-PLP and the sulfate ion, SepCysS should not bind Sep-tRNASec and discriminate tRNACys from tRNASec on the basis of the differences in the length of the T-arms, or SepCysS recognizes the discriminator sequence, which is Ura73 in tRNACys and Gua73 in tRNASec, overview
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additional information
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the highly conserved Cys residues Cys64, Cys67, and Cys272 are essential for the sulfhydrylation reaction in vivo. Cys64 and Cys67 form a disulfide linkage and carry a sulfane sulfur in a portion of the enzyme, suggesting that a persulfide group containing a sulfane sulfur is the proximal sulfur donor for cysteine biosynthesis. The presence of Cys272 increases the amount of sulfane sulfur in the enzyme by 3fold, suggesting that this Cys residue facilitates the generation of the persulfide group. A sulfur relay mechanism recruits both disulfide and persulfide intermediates
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additional information
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the highly conserved Cys residues Cys64, Cys67, and Cys272 are essential for the sulfhydrylation reaction in vivo. Cys64 and Cys67 form a disulfide linkage and carry a sulfane sulfur in a portion of the enzyme, suggesting that a persulfide group containing a sulfane sulfur is the proximal sulfur donor for cysteine biosynthesis. The presence of Cys272 increases the amount of sulfane sulfur in the enzyme by 3fold, suggesting that this Cys residue facilitates the generation of the persulfide group. A sulfur relay mechanism recruits both disulfide and persulfide intermediates
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additional information
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the highly conserved Cys residues Cys64, Cys67, and Cys272 are essential for the sulfhydrylation reaction in vivo. Cys64 and Cys67 form a disulfide linkage and carry a sulfane sulfur in a portion of the enzyme, suggesting that a persulfide group containing a sulfane sulfur is the proximal sulfur donor for cysteine biosynthesis. The presence of Cys272 increases the amount of sulfane sulfur in the enzyme by 3fold, suggesting that this Cys residue facilitates the generation of the persulfide group. A sulfur relay mechanism recruits both disulfide and persulfide intermediates
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additional information
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thiosulfate shows 72.6% of the activity compared to sulfide as sulfur donor, cysteine shows 77% of the activity compared to sulfide as sulfur donor. No correct Cys-tRNACys product is formed in presence of these sulfur donors
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additional information
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thiosulfate shows 72.6% of the activity compared to sulfide as sulfur donor, cysteine shows 77% of the activity compared to sulfide as sulfur donor. No correct Cys-tRNACys product is formed in presence of these sulfur donors
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