6.1.1.11: serine-tRNA ligase
This is an abbreviated version!
For detailed information about serine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.11
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6.1.1.11
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raman
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surface-enhanced
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nanoparticles
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silver
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aminoacyl-trna
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aminoacylation
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serylation
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colloid
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selenocysteine
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anticodon
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trnasec
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asprs
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isoacceptors
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aarss
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lysyl-trna
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roughened
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phenylalanyl-trna
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trnatyr
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langmuir-blodgett
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alanyl-trna
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handheld
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albomycins
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citrate-reduced
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molecular biology
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nanostars
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selenophosphate
- 6.1.1.11
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raman
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surface-enhanced
- nanoparticles
- silver
- aminoacyl-trna
- aminoacylation
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serylation
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colloid
- selenocysteine
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anticodon
- trnasec
- asprs
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isoacceptors
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aarss
- lysyl-trna
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roughened
- phenylalanyl-trna
- trnatyr
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langmuir-blodgett
- alanyl-trna
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handheld
- albomycins
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citrate-reduced
- molecular biology
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nanostars
- selenophosphate
Reaction
Synonyms
62 kDa RNA-binding protein, bacterial SerRS, bacterial type seryl-tRNA synthetase, bacterial-type SerRS, bMbSerRS, methanogenic SerRS, methanogenic type seryl-tRNA synthetase, methanogenic-type SerRS, methanogenic-type SerRSs, methanogenic-type seryl-tRNA synthetase, mMbSerRS, mSerRS, mtSerRS, SARS, SCSerS, Serine transfer RNA synthetase, Serine translase, Serine--tRNA ligase, SerRS, SerRS1, SerRS2, SerRSmt, serS, SERSEC, seryl tRNA synthetase, Seryl-transfer ribonucleate synthetase, Seryl-transfer ribonucleic acid synthetase, Seryl-transfer RNA synthetase, Seryl-tRNA synthetase, seryl-tRNA synthetase 1, seryl-tRNA synthetase 2, seryl-tRNA-synthetase, SerZMo, STS, subclass IIa dimeric SerRS, SvsR, Synthetase, seryl-transfer ribonucleate, tRNASer/seryl-tRNA synthetase, ttSerRS, TT_C0520, VlmL, ZmSerS
ECTree
6.1.1.11 serine-tRNA ligaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 6.1.1.11 - serine-tRNA ligase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-serine + tRNASec
AMP + diphosphate + L-seryl-tRNASec
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SerRS also aminoacylates tRNASec with serine as the first step for the incorporation of selenocysteine into proteins, SerRS is essential for growth Trypanosoma brucei and is responsible for the serylation of both tRNASer and tRNASec
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?
ATP + L-serine + tRNASec
AMP + diphosphate + L-seryl-tRNASec
SerRS also aminoacylates tRNASec with serine as the first step for the incorporation of selenocysteine into proteins, SerRS is responsible for the serylation of both tRNASer and tRNASec
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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-
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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gene silencing of the Nicotiana benthamiana SerRS causes severe leaf yellowing and abnormal leaf morphology, while maintaining almost normal plant growth. At the cell level depletion of the NcSRS gene results in dramatically reduced numbers of chloroplasts with reduced sizes and chlorophyll content. The numbers and/or physiology of mitochondria are also severely affected. The abnormal chloroplasts lack most of the thylakoid membranes and appear to be degenerating, whereas some of them show doublet morphology, indicating defective chloroplast division
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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-
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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r
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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r
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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r
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
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tRNASec, unlike most trypanosomal tRNAs, is exclusively localized in the cytosol, SerRS is essential for growth Trypanosoma brucei and is responsible for the serylation of both tRNASer and tRNASec
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
responsible for the serylation of both tRNASer and tRNASec
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?
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
tRNASer from Escherichia coli
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?
additional information
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high abundance in middle silk gland may result from an adaption of this organ for the production of the serine-rich protein, sericin
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?
additional information
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seryl-tRNA synthetase, MtSerRS, directly and stably interacts with arginyl-tRNA synthetase, MtArgRS, EC 6.1.1.19, two-hybrid system and surface plasmon resonance analysis, overview. The MtSerRS-MtArgRS complex also contains tRNAArg, consistent with the existence of a stable ribonucleoprotein complex active in aminoacylation. Deletion of the HTH motif, which contributes to the stability of SerRS dimers, significantly weakens the interaction between the two synthetases. Stimulation by MtArgRS peaks at 65°C
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additional information
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catalyzes the binding of 4-hydroxyaminoquinoline 1-oxide (a reduced metabolite of the carcinogenic and mutagenic compound 4-nitroquinoline 1-oxide) to nucleic acid. Seryl-tRNA synthetase may participate in vivo in the activation of some N-hydroxy compounds through their aminoacylation capacity
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?
additional information
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SerRS represents the housekeeping seryl-tRNA synthetase in the organism, one role of protein VlmL in valanimycin biosynthesis is to produce seryl-tRNA, which is then utilized for a subsequent step in the biosynthetic pathway, biosynthetic pathway for the antibiotic valanimycin, overview
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additional information
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SerRS represents the housekeeping seryl-tRNA synthetase in the organism, one role of protein VlmL in valanimycin biosynthesis is to produce seryl-tRNA, which is then utilized for a subsequent step in the biosynthetic pathway, biosynthetic pathway for the antibiotic valanimycin, overview
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?
