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Information on EC 2.5.1.73 - O-phospho-L-seryl-tRNA:Cys-tRNA synthase
for references in articles please use BRENDA:EC2.5.1.73
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EC Tree 2 Transferases
2.5 Transferring alkyl or aryl groups, other than methyl groups
2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
2.5.1.73 O-phospho-L-seryl-tRNA:Cys-tRNA synthase
IUBMB Comments
In organisms like Archaeoglobus fulgidus lacking EC 6.1.1.16 (cysteine—tRNA ligase) for the direct Cys-tRNACys formation, Cys-tRNACys is produced by an indirect pathway, in which EC 6.1.1.27 (O-phosphoseryl-tRNA ligase) ligates O-phosphoserine to tRNACys, and EC 2.5.1.73 converts the produced O-phospho-L-seryl-tRNACys to Cys-tRNACys. The SepRS/SepCysS pathway is the sole route for cysteine biosynthesis in the organism . Methanosarcina mazei can use both pathways, the direct route using EC 6.1.1.16 (cysteine—tRNA ligase) and the indirect pathway with EC 6.1.1.27 (O-phosphoseryl-tRNA ligase) and EC 2.5.1.73 .
The expected taxonomic range for this enzyme is: Archaea, Bacteria
- 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
showSynonyms
sepcyss, sep-trna:cys-trna synthase, sep-trna-cys-trna synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MJ1678
Sep-tRNA-Cys-tRNA synthase
both SepRS and SepCysS bind the reaction intermediate Sep-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-1alpha or infiltrating into the ribosome
Sep-tRNA:Cys-tRNA synthase
SepCysS
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
O-phospho-L-seryl-tRNACys + sulfide = L-cysteinyl-tRNACys + phosphate
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PATHWAY SOURCE
PATHWAYS
MetaCyc
L-cysteine biosynthesis II (tRNA-dependent)
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SYSTEMATIC NAME
IUBMB Comments
O-phospho-L-seryl-tRNACys:hydrogen sulfide 2-aminopropanoate transferase
In organisms like Archaeoglobus fulgidus lacking EC 6.1.1.16 (cysteine---tRNA ligase) for the direct Cys-tRNACys formation, Cys-tRNACys is produced by an indirect pathway, in which EC 6.1.1.27 (O-phosphoseryl-tRNA ligase) ligates O-phosphoserine to tRNACys, and EC 2.5.1.73 converts the produced O-phospho-L-seryl-tRNACys to Cys-tRNACys. The SepRS/SepCysS pathway is the sole route for cysteine biosynthesis in the organism [1]. Methanosarcina mazei can use both pathways, the direct route using EC 6.1.1.16 (cysteine---tRNA ligase) and the indirect pathway with EC 6.1.1.27 (O-phosphoseryl-tRNA ligase) and EC 2.5.1.73 [2].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
O-phospho-L-seryl-tRNASec + sulfide
L-cysteinyl-tRNASec + phosphate
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Substrates: 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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O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
Substrates: -
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O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
Substrates: evolutionary history of Cys-tRNACys formation, overview
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O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
Substrates: the in vivo sulfur donor is not determined
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O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
Substrates: -
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O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
Substrates: 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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Substrates: -
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O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
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Substrates: 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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Substrates: -
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O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
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Substrates: evolutionary history of Cys-tRNACys formation, overview
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
Substrates: -
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
Substrates: 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
Substrates: 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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Substrates: -
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
Substrates: -
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
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Substrates: 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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Substrates: sulfide e.g. from Na2S, anaerobic reaction
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
Substrates: 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
Substrates: 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
Substrates: 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
Substrates: 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
Substrates: 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
Substrates: 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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Substrates: 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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Substrates: 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
Substrates: 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
Substrates: SepCysS exhibits substrate preference among the three Methanosarcina mazei tRNACys isoacceptors
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additional information
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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
Substrates: evolutionary history of Cys-tRNACys formation, overview
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?
O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
Substrates: the in vivo sulfur donor is not determined
Products: -
Products: -
?
O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
Substrates: evolutionary history of Cys-tRNACys formation, overview
Products: -
Products: -
?
O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
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Substrates: evolutionary history of Cys-tRNACys formation, overview
Products: -
Products: -
?
O-phospho-L-seryl-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
-
Substrates: evolutionary history of Cys-tRNACys formation, overview
Products: -
Products: -
?
O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
-
Substrates: 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
Products: -
Products: -
?
O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
Substrates: 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
Products: -
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?
O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
Substrates: 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
Products: -
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O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
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Substrates: 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
Products: -
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additional information
?
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Substrates: 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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Substrates: 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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
dependent on, pyridoxal 5'-phosphate is covalently bound to the side-chain of the conserved Lys209 at the active site
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfate
is bound in the proximity of PLP by the side-chains of the conserved Arg79, His103, and Tyr104 residues, the PLP-bound active site is located deep within the large, basic cleft for recognizing Sep-tRNACys
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
translation factor SepCysE
essential for methanococcal Cys biosynthesis. Its deletion in Methanococcus maripaludiscauses Cys auxotrophy. SepCysE acts as a scaffold for O-phospho-L-serinetRNA ligase (EC 6.1.1.27) and O-phospho-L-seryl-tRNA:Cys-tRNA synthase to form a stable high-affinity complex for tRNACys causing a 14fold increase in the initial rate of Cys-tRNACys formation
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
highly sensitive assay to measure the activity of SepCysS under anaerobic conditions
additional information
highly sensitive assay to measure the activity of SepCysS under anaerobic conditions
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
wild-type enzyme can complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation
physiological function
the three domains of enhancer SepCysE each bind O-phosphoseryl-tRNA synthetase SepRS, Sep-tRNA:Cys-tRNA synthase SepCysS, and tRNACys, respectively, which mediates the dynamic architecture of the transsulfursome and enables a global long-range channeling of tRNACys between SepRS and SepCysS distant active sites
physiological function
-
wild-type enzyme can complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation
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physiological function
-
the three domains of enhancer SepCysE each bind O-phosphoseryl-tRNA synthetase SepRS, Sep-tRNA:Cys-tRNA synthase SepCysS, and tRNACys, respectively, which mediates the dynamic architecture of the transsulfursome and enables a global long-range channeling of tRNACys between SepRS and SepCysS distant active sites
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Show AA Sequence and Transmembrane Helices (618 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
dimer
the active site is located near the dimer interface, crystal structure analysis, overview
additional information
amino acid residue conservation mapping on the basis of the surface electrostatic potential, overview, construction of a SepRS-tRNACys-SepCysS ternary complex model, in the ternary complex the phosphoserylated 3'-terminus of tRNACys can possibly be transferred directly from SepRS to SepCysS, for conversion to the cysteinylated form, overview
additional information
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amino acid residue conservation mapping on the basis of the surface electrostatic potential, overview, construction of a SepRS-tRNACys-SepCysS ternary complex model, in the ternary complex the phosphoserylated 3'-terminus of tRNACys can possibly be transferred directly from SepRS to SepCysS, for conversion to the cysteinylated form, overview
additional information
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both SepRS and SepCysS are active as a monomer in theSepRSSepCysS binary complex
additional information
both SepRS and SepCysS are active as a monomer in theSepRSSepCysS binary complex
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type SepVysS1 and selenomethionine-labeled SepCysS1, hanging-drop vapor diffusion method, 0.001 ml protein solution is mixed with 0.001 ml reservoir solution containing 80 mM sodium acetate buffer, pH 4.4, 160 mM NaCl, and 1.00 M ammonium sulfate, 20°C, equilibration against 0.5 ml reservoir solution, cryoprotection by 25% v/v glycerol, X-ray diffraction structure determination and analysis at 2.4-3.2 A resolution, modeling
crystal structure of a subcomplex of the transsulfursome with tRNACys (SepCysS-SepCysE-tRNACys), which is involved in the second reaction step of the indirect pathway, to 2.6 A resolution. Space group P6522, with unit-cell parameters a = b = 107.2, c = 551.1 A. Two heterodimers of a synthase SepCysS dimer, an enhancer SepCysE dimer and one tRNACys are observed in the asymmetric unit
crystal structure of the complex of the enzyme with translation factor SepCysE, 2.8 A resolution
structure of the SepCysE-SepCysS-tRNACys ternary complex, at a resolution of 2.6 A by molecular replacement. SepCysS recognizes the discriminator base U73 of tRNACys
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C272A
loss of the ability to complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation
C64A
loss of the ability to complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation
C67A
loss of the ability to complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation
K234A
C272A
-
loss of the ability to complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation
-
C64A
-
loss of the ability to complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation
-
C67A
-
loss of the ability to complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation
-
additional information
additional information
active-site cysteine residues Cys39, Cys42 and Cys247 are essential for enzymic activity
additional information
-
active-site cysteine residues Cys39, Cys42 and Cys247 are essential for enzymic activity
additional information
the enzyme can synthesize Cys-tRNACys in a sepS deletion mutant when Na2S and O-phosphoserine are exogenously added, sepS encodes the O-phosphoseryl-tRNA synthetase, EC 6.1.1.B2
additional information
-
the enzyme can synthesize Cys-tRNACys in a sepS deletion mutant when Na2S and O-phosphoserine are exogenously added, sepS encodes the O-phosphoseryl-tRNA synthetase, EC 6.1.1.B2
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q Sepharose FF column chromatography and FPLC Mono Q column chromatography
recombinant SepCysS1 from Escherichia coli strain BL21(DE3) by anion exchange chromatography and affinity chromatography on a heparin resin, recombinant selenomethionine-labeled SepCysS1 from Escherichia coli strain B834
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Mj1678 or pscS, functional complementation of a cysteinyl-tRNACys synthase mutant strain, phylogenetic analysis, expression in Escherichia coli
-
phylogenetic analysis, overview
SepCysS1, overexpression in Escherichia coli strain BL21(DE3), expression of selenomethionine-labeled SepCysS1 in Escherichia coli strain B834
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fukunaga, R.; Yokoyama, S.
Structural insights into the second step of RNA-dependent cysteine biosynthesis in archaea: crystal structure of Sep-tRNA:Cys-tRNA synthase from Archaeoglobus fulgidus
J. Mol. Biol.
370
128-141
2007
Archaeoglobus fulgidus (O30207), Archaeoglobus fulgidus
brenda
O'Donoghue, P.; Sethi, A.; Woese, C.R.; Luthey-Schulten, Z.A.
The evolutionary history of Cys-tRNACys formation
Proc. Natl. Acad. Sci. USA
102
19003-19008
2005
Archaeoglobus fulgidus (O30207), Methanococcoides burtonii (Q12W26), Methanopyrus kandleri, Methanospirillum hungatei
brenda
Sauerwald, A.; Zhu, W.; Major, T.A.; Roy, H.; Palioura, S.; Jahn, D.; Whitman, W.B.; Yates, J.R.; Ibba, M.; Soell, D.
RNA-dependent cysteine biosynthesis in archea
Science
307
1969-1972
2005
Methanocaldococcus jannaschii, Methanococcus maripaludis (A4FWT8), Methanococcus maripaludis
brenda
Yuan, J.; Sheppard, K.; Soell, D.
Amino acid modifications on tRNA
Acta Biochim. Biophys. Sin. (Shanghai)
40
539-553
2008
Archaeoglobus fulgidus, Archaeoglobus fulgidus (O30207), Methanococcus maripaludis, no activity in Methanobrevibacter smithii, no activity in Methanosphaera stadtmanae
brenda
Hauenstein, S.I.; Perona, J.J.
Redundant synthesis of cysteinyl-tRNACys in Methanosarcina mazei
J. Biol. Chem.
283
22007-22017
2008
Methanosarcina mazei, Methanosarcina mazei (Q8PVS9)
brenda
Zhang, C.M.; Liu, C.; Slater, S.; Hou, Y.M.
Aminoacylation of tRNA with phosphoserine for synthesis of cysteinyl-tRNA(Cys)
Nat. Struct. Mol. Biol.
15
507-514
2008
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii (Q59072)
brenda
Yuan, J.; Hohn, M.J.; Sherrer, R.L.; Palioura, S.; Su, D.; Soell, D.
A tRNA-dependent cysteine biosynthesis enzyme recognizes the selenocysteine-specific tRNA in Escherichia coli
FEBS Lett.
584
2857-2861
2010
Escherichia coli
brenda
Helgadottir, S.; Sinapah, S.; Soell, D.; Ling, J.
Mutational analysis of Sep-tRNA:Cys-tRNA synthase reveals critical residues for tRNA-dependent cysteine formation
FEBS Lett.
586
60-63
2012
Methanocaldococcus jannaschii (Q59072), Methanocaldococcus jannaschii
brenda
Liu, Y.; Dos Santos, P.C.; Zhu, X.; Orlando, R.; Dean, D.R.; Soell, D.; Yuan, J.
Catalytic mechanism of Sep-tRNA:Cys-tRNA synthase: sulfur transfer is mediated by disulfide and persulfide
J. Biol. Chem.
287
5426-5433
2012
Methanocaldococcus jannaschii (Q59072), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q59072)
brenda
Liu, Y.; Nakamura, A.; Nakazawa, Y.; Asano, N.; Ford, K.A.; Hohn, M.J.; Tanaka, I.; Yao, M.; Sll, D.
Ancient translation factor is essential for tRNA-dependent cysteine biosynthesis in methanogenic archaea
Proc. Natl. Acad. Sci. USA
111
10520-10505
2014
Methanocaldococcus jannaschii (Q59072), Methanocaldococcus jannaschii DSM 2661 (Q59072)
brenda
Chen, M.; Nakazawa, Y.; Kubo, Y.; Asano, N.; Kato, K.; Tanaka, I.; Yao, M.
Crystallographic analysis of a subcomplex of the transsulfursome with tRNA for Cys-tRNACys synthesis
Acta Crystallogr. Sect. F
72
569-572
2016
Methanocaldococcus jannaschii (Q59072), Methanocaldococcus jannaschii DSM 2661 (Q59072)
brenda
Chen, M.; Kato, K.; Kubo, Y.; Tanaka, Y.; Liu, Y.; Long, F.; Whitman, W.B.; Lill, P.; Gatsogiannis, C.; Raunser, S.; Shimizu, N.; Shinoda, A.; Nakamura, A.; Tanaka, I.; Yao, M.
Structural basis for tRNA-dependent cysteine biosynthesis
Nat. Commun.
8
1521
2017
Methanocaldococcus jannaschii (Q59072), Methanocaldococcus jannaschii DSM 2661 (Q59072)
brenda
EXTERNAL LINKS (specific for EC-Number 2.5.1.73)
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Release 2023.1 (January 2023)
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