Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.5.1.73 - O-phospho-L-seryl-tRNA:Cys-tRNA synthase and Organism(s) Archaeoglobus fulgidus and UniProt Accession O30207

for references in articles please use BRENDA:EC2.5.1.73
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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 .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Archaeoglobus fulgidus
UNIPROT: O30207
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
sepcyss, sep-trna:cys-trna synthase, sep-trna-cys-trna synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Sep-tRNA:Cys-tRNA synthase
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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].
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-tRNACys + sulfide
L-cysteinyl-tRNACys + phosphate
show the reaction diagram
the sulfur donor for this enzyme is unknown though in vitro sulfide is sufficient
-
-
?
additional information
?
-
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-tRNACys + sulfate
L-cysteinyl-tRNACys + phosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
phylogenetic analysis, overview
SepCysS1, overexpression in Escherichia coli strain BL21(DE3), expression of selenomethionine-labeled SepCysS1 in Escherichia coli strain B834
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team