Information on EC 2.5.1.73 - O-phospho-L-seryl-tRNA:Cys-tRNA synthase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
2.5.1.73
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RECOMMENDED NAME
GeneOntology No.
O-phospho-L-seryl-tRNA:Cys-tRNA synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
O-phospho-L-seryl-tRNACys + sulfide = L-cysteinyl-tRNACys + phosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-cysteine biosynthesis II (tRNA-dependent)
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Aminoacyl-tRNA biosynthesis
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SepCysS1; SepCysS1
SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
two genes
SwissProt
Manually annotated by BRENDA team
no activity in Methanobrevibacter smithii
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Manually annotated by BRENDA team
no activity in Methanosphaera stadtmanae
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
show the reaction diagram
O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
show the reaction diagram
O-phospho-L-seryl-tRNASec + sulfide
L-cysteinyl-tRNASec + phosphate
show the reaction diagram
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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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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
show the reaction diagram
O-phospho-L-seryl-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
translation factor SepCysE
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essential for methanococcal Cys biosynthesis. Its deletion in Methanococcus maripaludiscauses Cys auxotrophy. SepCysE acts as a scaffold for O-phospho-L-serine—tRNA 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 hide
LITERATURE
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
84000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 42000, gel filtration; 2 * 42324, predicted from amino acid sequence
additional information
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 the complex of the enzyme with translation factor SepCysE, 2.8 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; DEAE column chromatography and Superdex 200 gel filtration
native enzyme to homogeneity
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Q Sepharose FF column chromatography and FPLC Mono Q column chromatography
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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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)-RIL cells
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expressed in Escherichia coli Rosetta2(DE3) pLysS cells; expression in Escherichia coli
expression in Escherchia coli
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gene Mj1678 or pscS, functional complementation of a cysteinyl-tRNACys synthase mutant strain, phylogenetic analysis, expression in Escherichia coli
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phylogenetic analysis, overview
SepCysS1, overexpression in Escherichia coli strain BL21(DE3), expression of selenomethionine-labeled SepCysS1 in Escherichia coli strain B834
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C113A
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activity similar to wild-type
C209A
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activity similar to wild-type
C272A
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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
C272S
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complete loss of activity
C64A
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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
C64S
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complete loss of activity
C67A
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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
C67S
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complete loss of activity
D182A
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107% of wild-type activity
H126A
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complete loss of activity
H233A
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complete loss of activity
H325A
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124% of wild-type activity
K265A
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complete loss of activity
K354A/R356A
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92% of wild-type activity
K370A
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33% of wild-type activity
N187A
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85% of wild-type activity
N208A
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101% of wild-type activity
R102A
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complete loss of activity
R292A
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99% of wild-type activity
R96A
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89% of wild-type activity
S231A
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complete loss of activity
Y127A
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35% of wild-type activity
C113A
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activity similar to wild-type
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C272A
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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
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C64A
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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
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C67A
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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
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K234A
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complete loss of activtiy
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additional information
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