Information on EC 2.9.1.1 - L-seryl-tRNASec selenium transferase

for references in articles please use BRENDA:EC2.9.1.1
Word Map on EC 2.9.1.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


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

EC NUMBER
COMMENTARY hide
2.9.1.1
-
RECOMMENDED NAME
GeneOntology No.
L-seryl-tRNASec selenium transferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-seryl-tRNASec + selenophosphate = L-selenocysteinyl-tRNASec + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Selenium transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-selenocysteine biosynthesis I (bacteria)
-
-
selenocysteine biosynthesis
-
-
Selenocompound metabolism
-
-
Aminoacyl-tRNA biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
selenophosphate:L-seryl-tRNASec selenium transferase
A pyridoxal 5'-phosphate enzyme identified in Escherichia coli. Recognises specifically tRNASec-species. Binding of tRNASec also occurs in the absence of the seryl group. 2-Aminoacryloyl-tRNA, bound to the enzyme as an imine with the pyridoxal phosphate, is an intermediate in the reaction. Since the selenium atom replaces oxygen in serine, the product may also be referred to as L-selenoseryl-tRNASec. The symbol Sel has also been used for selenocysteine but Sec is preferred.
CAS REGISTRY NUMBER
COMMENTARY hide
183869-06-9
-
211752-49-7
synthase, selenocysteine (Moorella thermoacetica clone pCTA100/pCTAB1 gene selA) /GenBank Y14814-derived protein GI 2440135 /selenocysteine synthase (Moorella thermoacetica strain DSM521 clone pCTA 100/pCTAB1 gene selA)
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
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
L-Seryl-tRNASec + selenide
?
show the reaction diagram
-
active only at much higher concentrations than those of the selenophosphate
-
-
-
L-Seryl-tRNASec + selenophosphate
?
show the reaction diagram
-
the enzyme is involved in the biosynthesis of selenocysteine
-
-
-
L-Seryl-tRNASec + selenophosphate
L-Selenocysteinyl-tRNASec + H2O + phosphate
show the reaction diagram
L-seryl-tRNASec + selenophosphate
L-selenocysteinyl-tRNASec + phosphate
show the reaction diagram
L-Seryl-tRNASec + sulfide
?
show the reaction diagram
-
active only at much higher concentrations than those of the thiophosphate
-
-
-
L-Seryl-tRNASec + thiophosphate
Cysteyl-tRNASec + H2O + phosphate
show the reaction diagram
-
-
-
-
seryl-tRNASec + monoselenophosphate
selenocysteinyl-tRNASec + H2O + phosphate
show the reaction diagram
-
selenoamino acid metabolism
-
-
?
seryl-tRNASec + selenophosphate
selenocysteinyl-tRNASec + H2O + phosphate
show the reaction diagram
additional information
?
-
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
L-Seryl-tRNASec + selenophosphate
?
show the reaction diagram
-
the enzyme is involved in the biosynthesis of selenocysteine
-
-
-
L-seryl-tRNASec + selenophosphate
L-selenocysteinyl-tRNASec + phosphate
show the reaction diagram
seryl-tRNASec + monoselenophosphate
selenocysteinyl-tRNASec + H2O + phosphate
show the reaction diagram
-
selenoamino acid metabolism
-
-
?
seryl-tRNASec + selenophosphate
selenocysteinyl-tRNASec + H2O + phosphate
show the reaction diagram
-
selenoamino acid metabolism
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
potassium borohydride
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0003
Selenophosphate
-
-
0.004
thiophosphate
-
-
additional information
additional information
-
kinetics study of selenocysteine incorporation
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0217
Selenophosphate
-
-
0.000867
thiophosphate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
-
about, gel filtration
49000
-
4 * 49000, SDS-PAGE
50667
-
x * 50667, calculation from nucleotide sequence
52500
-
calculated from amino acid sequence
600000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
-
the homodecamer has a ring-like structure with five bilobed wings, similar to the structure of the Escherichia coli complex
homodecamer
tetramer
-
4 * 49000, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apoenzyme and in complex with Thermoanaerobacter tengcongensis tRNASec, vapor diffusion method
purified recombinant C-terminally His6-tagged SecS, apoenzyme or in complex with phosphate or iodide, sitting-drop vapor diffusion at 20°C, 14 mg/ml protein in 10 mM HEPES-NaOH, pH 7.5, 500 mM NaCl, 2 mM DTT, is mixed with an equal volume of reservoir solution containing 11% v/v ethylene glycol without other buffer components, 2 days, cryoprotection by crystal soaking in 100 mM HEPES-NaOH, pH 7.5, 250 mM NaCl, 1 mM dithiothreitol, and 35% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 1.65-2.38 A resolution
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
the protein stability is maintained up to 45°C. The enzyme has a thermal transition from 60 to 70°C with a melting temperature of 66°C and an evident plateau above 70°C, in which all secondary structures are lost and the protein is completely denatured
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, hydroxyapatite column chromatography, Hi Trap Q column chromatography, and Superdex 200 gel filtration
-
centrifugation at 150000 xg, followed by succesive chromatography of the supernatant on DEAE-cellulose, Sephacryl S-300 and Heparin-Toyopearl
-
recombinant C-terminally His6-tagged SecS from Escherichia coli strain Rosetta2(DE3) by nickel affinity chromatography and gel filtration to over 95% purity
-
recombinant SelA from Escherichia coli strain DH5alpha by anion exchange chromatography, ammonium sulfate fractionation, and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain WL81460
-
expressed in Escherichia coli WL81460 (lambdaDE3) cells
-
expression of SecS as C-terminally His6-tagged enzyme in Escherichia coli strain Rosetta2(DE3)
-
gene secS, DNA and amino acid sequence determination and analysis
-
selA, expression in Escherichia coli strain DH5alpha
-
Show AA Sequence (5640 entries)
Longer loading times are possible. Please use the Sequence Search for a specific query.