UniProtKB - P0AGJ9 (SYY_ECOLI)
Protein
Tyrosine--tRNA ligase
Gene
tyrS
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) (PubMed:4292198, PubMed:4579631). Can also mischarge tRNA(Tyr) with D-tyrosine, leading to the formation of D-tyrosyl-tRNA(Tyr), which can be hydrolyzed by the D-aminoacyl-tRNA deacylase (PubMed:4292198). In vitro, can also use the non-natural amino acid azatyrosine (PubMed:11006270).3 Publications
Catalytic activityi
- ATP + L-tyrosine + tRNATyr = AMP + diphosphate + H+ + L-tyrosyl-tRNATyrUniRule annotation4 PublicationsEC:6.1.1.1UniRule annotation4 Publications
Activity regulationi
Magnesium is essential for activity (PubMed:4579631). Inhibited by chloride and sulfate in the presence of 1 mM free Mg2+. When the Mg2+ concentration increases to 10 mM there is almost no chloride inhibition any more. Inhibited by diphosphate and AMP. Chloride strengthens the diphosphate inhibition and weakens the AMP inhibition. Chloride weakens the binding of Mg2+ to the RNA and thereby the interaction between the enzyme and the RNA (PubMed:10572925). Acetylation at certain lysine residues could significantly impair activity (PubMed:28741290). D-tyrosine is a competitive inhibitor of L-tyrosine for the formation of tyrosyl-tRNA(Tyr) (PubMed:4292198).4 Publications
Kineticsi
kcat is 0.74 sec(-1) with L-tyrosine as substrate. kcat is 0.11 sec(-1) with azatyrosine as substrate.1 Publication
- KM=0.027 mM for L-tyrosine1 Publication
- KM=0.0033 mM for L-tyrosine1 Publication
- KM=0.015 mM for D-tyrosine1 Publication
- KM=0.0177 mM for azatyrosine1 Publication
- KM=22 nM for tRNA(Tyr) (in the absence of KCl)1 Publication
- KM=37 nM for tRNA(Tyr) (in the presence of 50 mM KCl)1 Publication
- KM=93 nM for tRNA(Tyr) (in the presence of 100 mM KCl)1 Publication
- KM=240 nM for tRNA(Tyr) (in the presence of 150 mM KCl)1 Publication
- Vmax=2.6 µmol/min/mg enzyme for L-tyrosine1 Publication
- Vmax=0.11 µmol/min/mg enzyme for D-tyrosine1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 37 | TyrosineUniRule annotation1 Publication1 Publication | 1 | |
Binding sitei | 175 | TyrosineUniRule annotation1 Publication2 Publications | 1 | |
Binding sitei | 179 | TyrosineUniRule annotation1 Publication2 Publications | 1 | |
Binding sitei | 198 | Tyr-AMP intermediate adenyl group; via amide nitrogen | 1 | |
Binding sitei | 200 | Tyr-AMP intermediate adenyl group | 1 | |
Binding sitei | 228 | Tyr-AMP intermediate adenyl group; via amide nitrogen and carbonyl oxygen | 1 | |
Sitei | 231 | Cross-linked with tRNA by periodate oxidation | 1 | |
Sitei | 235 | Cross-linked with tRNA by periodate oxidation; predominant | 1 | |
Binding sitei | 238 | ATPUniRule annotation | 1 | |
Sitei | 238 | Cross-linked with tRNA by periodate oxidation | 1 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-UniRule
- RNA binding Source: UniProtKB-KW
- tyrosine-tRNA ligase activity Source: EcoCyc
GO - Biological processi
- tRNA aminoacylation Source: GO_Central
- tyrosyl-tRNA aminoacylation Source: EcoCyc
Keywordsi
Molecular function | Aminoacyl-tRNA synthetase, Ligase, RNA-binding |
Biological process | Protein biosynthesis |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:TYRS-MONOMER MetaCyc:TYRS-MONOMER |
BRENDAi | 6.1.1.1, 2026 |
SABIO-RKi | P0AGJ9 |
Names & Taxonomyi
Protein namesi | Recommended name: Tyrosine--tRNA ligaseUniRule annotationCurated (EC:6.1.1.1UniRule annotation4 Publications)Alternative name(s): Tyrosyl-tRNA synthetase1 PublicationUniRule annotation Short name: TyrRS1 PublicationUniRule annotation |
Gene namesi | Name:tyrS1 Publication Ordered Locus Names:b1637, JW1629 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotationCurated
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Biotechnological usei
Utilization for in vivo protein biosynthesis of mutants that charge azatyrosine efficiently to tRNA may lead to efficient production of azatyrosine-containing alloproteins, which have immense potential in biotechnology and medicine.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 37 | Y → V: Confers specificity for the non-natural amino acid 3-iodo-tyrosine; when associated with C-195. 1 Publication | 1 | |
Mutagenesisi | 130 | F → S: Utilizes the non-natural amino acid azatyrosine more efficiently than tyrosine. Strong decrease in affinity for tyrosine and small increase in affinity for azatyrosine. Temperature-sensitive. 1 Publication | 1 | |
Mutagenesisi | 195 | Q → C: Confers specificity for the non-natural amino acid 3-iodo-tyrosine; when associated with V-37. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL4295572 |
DrugBanki | DB01758, 3-Iodo-Tyrosine DB03325, Tyrosyladenylate |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000055652 | 2 – 424 | Tyrosine--tRNA ligaseAdd BLAST | 423 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 144 | N6-acetyllysine1 Publication | 1 |
Post-translational modificationi
Acetylated at Lys-144 (PubMed:18723842, PubMed:28741290). Acetylation at Lys-144 leads to slightly decreased activity (PubMed:28741290). In vitro, in the presence of acetyl-phosphate, can also be acetylated at Lys-67, Lys-85, Lys-90, Lys-230, Lys-235, Lys-238, Lys-321 and Lys-377. Acetylation at Lys-85, Lys-235 or Lys-238 causes dramatic decrease in activity (PubMed:28741290).2 Publications
Keywords - PTMi
AcetylationProteomic databases
jPOSTi | P0AGJ9 |
PaxDbi | P0AGJ9 |
PRIDEi | P0AGJ9 |
2D gel databases
SWISS-2DPAGEi | P0AGJ9 |
PTM databases
iPTMneti | P0AGJ9 |
Interactioni
Subunit structurei
Protein-protein interaction databases
BioGRIDi | 4263487, 47 interactors |
DIPi | DIP-36227N |
IntActi | P0AGJ9, 8 interactors |
STRINGi | 511145.b1637 |
Chemistry databases
BindingDBi | P0AGJ9 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0AGJ9 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0AGJ9 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 357 – 414 | S4 RNA-bindingPROSITE-ProRule annotationAdd BLAST | 58 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 42 – 51 | 'HIGH' regionUniRule annotation | 10 | |
Motifi | 235 – 239 | 'KMSKS' regionUniRule annotation | 5 |
Sequence similaritiesi
Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily.UniRule annotationCurated
Phylogenomic databases
eggNOGi | COG0162, Bacteria |
InParanoidi | P0AGJ9 |
PhylomeDBi | P0AGJ9 |
Family and domain databases
CDDi | cd00165, S4, 1 hit cd00805, TyrRS_core, 1 hit |
Gene3Di | 3.10.290.10, 1 hit 3.40.50.620, 1 hit |
HAMAPi | MF_02006, Tyr_tRNA_synth_type1, 1 hit |
InterProi | View protein in InterPro IPR001412, aa-tRNA-synth_I_CS IPR002305, aa-tRNA-synth_Ic IPR014729, Rossmann-like_a/b/a_fold IPR002942, S4_RNA-bd IPR036986, S4_RNA-bd_sf IPR002307, Tyr-tRNA-ligase IPR024088, Tyr-tRNA-ligase_bac-type IPR024107, Tyr-tRNA-ligase_bac_1 |
PANTHERi | PTHR11766, PTHR11766, 1 hit |
Pfami | View protein in Pfam PF01479, S4, 1 hit PF00579, tRNA-synt_1b, 1 hit |
PRINTSi | PR01040, TRNASYNTHTYR |
SMARTi | View protein in SMART SM00363, S4, 1 hit |
TIGRFAMsi | TIGR00234, tyrS, 1 hit |
PROSITEi | View protein in PROSITE PS00178, AA_TRNA_LIGASE_I, 1 hit PS50889, S4, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0AGJ9-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MASSNLIKQL QERGLVAQVT DEEALAERLA QGPIALYCGF DPTADSLHLG
60 70 80 90 100
HLVPLLCLKR FQQAGHKPVA LVGGATGLIG DPSFKAAERK LNTEETVQEW
110 120 130 140 150
VDKIRKQVAP FLDFDCGENS AIAANNYDWF GNMNVLTFLR DIGKHFSVNQ
160 170 180 190 200
MINKEAVKQR LNREDQGISF TEFSYNLLQG YDFACLNKQY GVVLQIGGSD
210 220 230 240 250
QWGNITSGID LTRRLHQNQV FGLTVPLITK ADGTKFGKTE GGAVWLDPKK
260 270 280 290 300
TSPYKFYQFW INTADADVYR FLKFFTFMSI EEINALEEED KNSGKAPRAQ
310 320 330 340 350
YVLAEQVTRL VHGEEGLQAA KRITECLFSG SLSALSEADF EQLAQDGVPM
360 370 380 390 400
VEMEKGADLM QALVDSELQP SRGQARKTIA SNAITINGEK QSDPEYFFKE
410 420
EDRLFGRFTL LRRGKKNYCL ICWK
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J01719 Genomic DNA Translation: AAA24707.1 U00096 Genomic DNA Translation: AAC74709.1 AP009048 Genomic DNA Translation: BAA15398.1 M92351 Genomic DNA Translation: AAA24710.1 |
PIRi | A01178, SYECYT |
RefSeqi | NP_416154.1, NC_000913.3 WP_001295400.1, NZ_STEB01000003.1 |
Genome annotation databases
EnsemblBacteriai | AAC74709; AAC74709; b1637 BAA15398; BAA15398; BAA15398 |
GeneIDi | 57731032 948855 |
KEGGi | ecj:JW1629 eco:b1637 |
PATRICi | fig|1411691.4.peg.623 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J01719 Genomic DNA Translation: AAA24707.1 U00096 Genomic DNA Translation: AAC74709.1 AP009048 Genomic DNA Translation: BAA15398.1 M92351 Genomic DNA Translation: AAA24710.1 |
PIRi | A01178, SYECYT |
RefSeqi | NP_416154.1, NC_000913.3 WP_001295400.1, NZ_STEB01000003.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1VBM | X-ray | 2.70 | A/B | 5-322 | [»] | |
1VBN | X-ray | 2.70 | A/B | 5-322 | [»] | |
1WQ3 | X-ray | 2.00 | A | 1-322 | [»] | |
1WQ4 | X-ray | 2.00 | A | 2-322 | [»] | |
1X8X | X-ray | 2.00 | A | 1-322 | [»] | |
2YXN | X-ray | 1.80 | A | 1-322 | [»] | |
6HB5 | X-ray | 1.88 | A/B | 1-424 | [»] | |
6HB6 | X-ray | 1.92 | A/B | 1-424 | [»] | |
6HB7 | X-ray | 1.90 | A/B | 1-424 | [»] | |
6I5Y | X-ray | 1.90 | A/B | 1-424 | [»] | |
6WN2 | X-ray | 1.78 | A/B | 1-322 | [»] | |
7AP3 | X-ray | 2.00 | A/B | 1-424 | [»] | |
SMRi | P0AGJ9 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263487, 47 interactors |
DIPi | DIP-36227N |
IntActi | P0AGJ9, 8 interactors |
STRINGi | 511145.b1637 |
Chemistry databases
BindingDBi | P0AGJ9 |
ChEMBLi | CHEMBL4295572 |
DrugBanki | DB01758, 3-Iodo-Tyrosine DB03325, Tyrosyladenylate |
PTM databases
iPTMneti | P0AGJ9 |
2D gel databases
SWISS-2DPAGEi | P0AGJ9 |
Proteomic databases
jPOSTi | P0AGJ9 |
PaxDbi | P0AGJ9 |
PRIDEi | P0AGJ9 |
Genome annotation databases
EnsemblBacteriai | AAC74709; AAC74709; b1637 BAA15398; BAA15398; BAA15398 |
GeneIDi | 57731032 948855 |
KEGGi | ecj:JW1629 eco:b1637 |
PATRICi | fig|1411691.4.peg.623 |
Organism-specific databases
EchoBASEi | EB1036 |
Phylogenomic databases
eggNOGi | COG0162, Bacteria |
InParanoidi | P0AGJ9 |
PhylomeDBi | P0AGJ9 |
Enzyme and pathway databases
BioCyci | EcoCyc:TYRS-MONOMER MetaCyc:TYRS-MONOMER |
BRENDAi | 6.1.1.1, 2026 |
SABIO-RKi | P0AGJ9 |
Miscellaneous databases
EvolutionaryTracei | P0AGJ9 |
PROi | PR:P0AGJ9 |
Family and domain databases
CDDi | cd00165, S4, 1 hit cd00805, TyrRS_core, 1 hit |
Gene3Di | 3.10.290.10, 1 hit 3.40.50.620, 1 hit |
HAMAPi | MF_02006, Tyr_tRNA_synth_type1, 1 hit |
InterProi | View protein in InterPro IPR001412, aa-tRNA-synth_I_CS IPR002305, aa-tRNA-synth_Ic IPR014729, Rossmann-like_a/b/a_fold IPR002942, S4_RNA-bd IPR036986, S4_RNA-bd_sf IPR002307, Tyr-tRNA-ligase IPR024088, Tyr-tRNA-ligase_bac-type IPR024107, Tyr-tRNA-ligase_bac_1 |
PANTHERi | PTHR11766, PTHR11766, 1 hit |
Pfami | View protein in Pfam PF01479, S4, 1 hit PF00579, tRNA-synt_1b, 1 hit |
PRINTSi | PR01040, TRNASYNTHTYR |
SMARTi | View protein in SMART SM00363, S4, 1 hit |
TIGRFAMsi | TIGR00234, tyrS, 1 hit |
PROSITEi | View protein in PROSITE PS00178, AA_TRNA_LIGASE_I, 1 hit PS50889, S4, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | SYY_ECOLI | |
Accessioni | P0AGJ9Primary (citable) accession number: P0AGJ9 Secondary accession number(s): P00951 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | January 23, 2007 | |
Last modified: | April 7, 2021 | |
This is version 133 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Aminoacyl-tRNA synthetases
List of aminoacyl-tRNA synthetase entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families