Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tyrosine--tRNA ligase

Gene

tyrS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of 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).

Catalytic activityi

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei37 – 371Tyrosine1 Publication
Binding sitei175 – 1751Tyrosine1 Publication
Binding sitei179 – 1791Tyrosine1 Publication
Binding sitei198 – 1981Tyr-AMP intermediate adenyl group; via amide nitrogen
Binding sitei200 – 2001Tyr-AMP intermediate adenyl group
Binding sitei228 – 2281Tyr-AMP intermediate adenyl group; via amide nitrogen and carbonyl oxygen
Sitei231 – 2311Cross-linked with tRNA by periodate oxidation
Sitei235 – 2351Cross-linked with tRNA by periodate oxidation; predominant
Binding sitei238 – 2381ATPBy similarity
Sitei238 – 2381Cross-linked with tRNA by periodate oxidation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-HAMAP
  • RNA binding Source: UniProtKB-KW
  • tyrosine-tRNA ligase activity Source: EcoCyc

GO - Biological processi

  • tRNA aminoacylation Source: GO_Central
  • tyrosyl-tRNA aminoacylation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:TYRS-MONOMER.
ECOL316407:JW1629-MONOMER.
MetaCyc:TYRS-MONOMER.
BRENDAi6.1.1.1. 2026.
SABIO-RKP0AGJ9.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine--tRNA ligase (EC:6.1.1.1)
Alternative name(s):
Tyrosyl-tRNA synthetase
Short name:
TyrRS
Gene namesi
Name:tyrS
Ordered Locus Names:b1637, JW1629
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11043. tyrS.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi37 – 371Y → V: Confers specificity for the non-natural amino acid 3-iodo-tyrosine; when associated with C-195.
Mutagenesisi195 – 1951Q → C: Confers specificity for the non-natural amino acid 3-iodo-tyrosine; when associated with V-37.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 424423Tyrosine--tRNA ligasePRO_0000055652Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei144 – 1441N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0AGJ9.
PaxDbiP0AGJ9.
PRIDEiP0AGJ9.

2D gel databases

SWISS-2DPAGEP0AGJ9.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi4263487. 17 interactions.
DIPiDIP-36227N.
IntActiP0AGJ9. 8 interactions.
MINTiMINT-1224558.
STRINGi511145.b1637.

Structurei

Secondary structure

1
424
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 127Combined sources
Beta strandi17 – 215Combined sources
Helixi22 – 3110Combined sources
Beta strandi35 – 406Combined sources
Beta strandi43 – 464Combined sources
Helixi49 – 6315Combined sources
Beta strandi67 – 726Combined sources
Helixi76 – 783Combined sources
Helixi94 – 10815Combined sources
Helixi109 – 1113Combined sources
Beta strandi114 – 1163Combined sources
Helixi117 – 1193Combined sources
Beta strandi122 – 1254Combined sources
Helixi127 – 1304Combined sources
Helixi135 – 1417Combined sources
Helixi143 – 1453Combined sources
Helixi148 – 1514Combined sources
Helixi155 – 1628Combined sources
Helixi164 – 1663Combined sources
Helixi170 – 1734Combined sources
Helixi175 – 19016Combined sources
Beta strandi192 – 1976Combined sources
Helixi199 – 2013Combined sources
Helixi202 – 21615Combined sources
Beta strandi221 – 2244Combined sources
Beta strandi240 – 2423Combined sources
Beta strandi245 – 2473Combined sources
Turni248 – 2503Combined sources
Helixi253 – 2619Combined sources
Helixi265 – 27511Combined sources
Helixi280 – 29314Combined sources
Helixi299 – 31921Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VBMX-ray2.70A/B5-322[»]
1VBNX-ray2.70A/B5-322[»]
1WQ3X-ray2.00A1-322[»]
1WQ4X-ray2.00A2-322[»]
1X8XX-ray2.00A1-322[»]
2YXNX-ray1.80A1-322[»]
ProteinModelPortaliP0AGJ9.
SMRiP0AGJ9. Positions 1-424.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AGJ9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini357 – 41458S4 RNA-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi42 – 5110"HIGH" region
Motifi235 – 2395"KMSKS" region

Sequence similaritiesi

Contains 1 S4 RNA-binding domain.Curated

Phylogenomic databases

eggNOGiENOG4105DA0. Bacteria.
COG0162. LUCA.
HOGENOMiHOG000242790.
InParanoidiP0AGJ9.
KOiK01866.
OMAiGKHFPVN.
OrthoDBiEOG6B09VR.
PhylomeDBiP0AGJ9.

Family and domain databases

Gene3Di3.10.290.10. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_02006. Tyr_tRNA_synth_type1.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002942. S4_RNA-bd.
IPR002307. Tyr-tRNA-ligase.
IPR024088. Tyr-tRNA-ligase_bac-type.
IPR024107. Tyr-tRNA-ligase_bac_1.
[Graphical view]
PANTHERiPTHR11766. PTHR11766. 1 hit.
PfamiPF01479. S4. 1 hit.
PF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSiPR01040. TRNASYNTHTYR.
SMARTiSM00363. S4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00234. tyrS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AGJ9-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:424
Mass (Da):47,527
Last modified:January 23, 2007 - v2
Checksum:i98E7080D85B356A2
GO

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.
PIRiA01178. SYECYT.
RefSeqiNP_416154.1. NC_000913.3.
WP_001295400.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74709; AAC74709; b1637.
BAA15398; BAA15398; BAA15398.
GeneIDi948855.
KEGGiecj:JW1629.
eco:b1637.
PATRICi32118576. VBIEscCol129921_1708.

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.
PIRiA01178. SYECYT.
RefSeqiNP_416154.1. NC_000913.3.
WP_001295400.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VBMX-ray2.70A/B5-322[»]
1VBNX-ray2.70A/B5-322[»]
1WQ3X-ray2.00A1-322[»]
1WQ4X-ray2.00A2-322[»]
1X8XX-ray2.00A1-322[»]
2YXNX-ray1.80A1-322[»]
ProteinModelPortaliP0AGJ9.
SMRiP0AGJ9. Positions 1-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263487. 17 interactions.
DIPiDIP-36227N.
IntActiP0AGJ9. 8 interactions.
MINTiMINT-1224558.
STRINGi511145.b1637.

2D gel databases

SWISS-2DPAGEP0AGJ9.

Proteomic databases

EPDiP0AGJ9.
PaxDbiP0AGJ9.
PRIDEiP0AGJ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74709; AAC74709; b1637.
BAA15398; BAA15398; BAA15398.
GeneIDi948855.
KEGGiecj:JW1629.
eco:b1637.
PATRICi32118576. VBIEscCol129921_1708.

Organism-specific databases

EchoBASEiEB1036.
EcoGeneiEG11043. tyrS.

Phylogenomic databases

eggNOGiENOG4105DA0. Bacteria.
COG0162. LUCA.
HOGENOMiHOG000242790.
InParanoidiP0AGJ9.
KOiK01866.
OMAiGKHFPVN.
OrthoDBiEOG6B09VR.
PhylomeDBiP0AGJ9.

Enzyme and pathway databases

BioCyciEcoCyc:TYRS-MONOMER.
ECOL316407:JW1629-MONOMER.
MetaCyc:TYRS-MONOMER.
BRENDAi6.1.1.1. 2026.
SABIO-RKP0AGJ9.

Miscellaneous databases

EvolutionaryTraceiP0AGJ9.
PROiP0AGJ9.

Family and domain databases

Gene3Di3.10.290.10. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_02006. Tyr_tRNA_synth_type1.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002942. S4_RNA-bd.
IPR002307. Tyr-tRNA-ligase.
IPR024088. Tyr-tRNA-ligase_bac-type.
IPR024107. Tyr-tRNA-ligase_bac_1.
[Graphical view]
PANTHERiPTHR11766. PTHR11766. 1 hit.
PfamiPF01479. S4. 1 hit.
PF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSiPR01040. TRNASYNTHTYR.
SMARTiSM00363. S4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00234. tyrS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The tyrosyl-tRNA synthetase from Escherichia coli. Complete nucleotide sequence of the structural gene."
    Barker D.G., Bruton C.J., Winter G.
    FEBS Lett. 150:419-423(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Characterization of the complex pdxH-tyrS operon of Escherichia coli K-12 and pleiotropic phenotypes caused by pdxH insertion mutations."
    Lam H.-M., Winkler M.E.
    J. Bacteriol. 174:6033-6045(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
    Strain: K12.
  6. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  7. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-144, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  8. "Structural snapshots of the KMSKS loop rearrangement for amino acid activation by bacterial tyrosyl-tRNA synthetase."
    Kobayashi T., Takimura T., Sekine R., Vincent K., Kamata K., Sakamoto K., Nishimura S., Yokoyama S.
    J. Mol. Biol. 346:105-117(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-322 IN COMPLEX WITH TYROSINE AND TYR-AMP ANALOG.
  9. "Structural basis of nonnatural amino acid recognition by an engineered aminoacyl-tRNA synthetase for genetic code expansion."
    Kobayashi T., Sakamoto K., Takimura T., Sekine R., Kelly V.P., Kamata K., Nishimura S., Yokoyama S.
    Proc. Natl. Acad. Sci. U.S.A. 102:1366-1371(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-322 OF MUTANT VAL-37/CYS-195 IN COMPLEX WITH SUBSTRATE, SUBUNIT.

Entry informationi

Entry nameiSYY_ECOLI
AccessioniPrimary (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: March 16, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.