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Protein

Aspartate--tRNA ligase

Gene

aspS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of glutamate to tRNA(Asp) in a two-step reaction: aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).UniRule annotation

Catalytic activityi

ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei171 – 1711AspartateUniRule annotation
Binding sitei217 – 2171AspartateUniRule annotation
Binding sitei226 – 2261ATPUniRule annotation
Binding sitei448 – 4481AspartateUniRule annotation
Binding sitei482 – 4821ATPUniRule annotation
Binding sitei489 – 4891AspartateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi217 – 2193ATPUniRule annotation
Nucleotide bindingi534 – 5374ATPUniRule annotation

GO - Molecular functioni

  • aspartate-tRNA ligase activity Source: EcoCyc
  • ATP binding Source: UniProtKB-KW
  • nucleic acid binding Source: InterPro

GO - Biological processi

  • aspartyl-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

Enzyme and pathway databases

BioCyciEcoCyc:ASPS-MONOMER.
ECOL316407:JW1855-MONOMER.
MetaCyc:ASPS-MONOMER.
BRENDAi6.1.1.12. 2026.
SABIO-RKP21889.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate--tRNA ligaseUniRule annotation (EC:6.1.1.12UniRule annotation)
Alternative name(s):
Aspartyl-tRNA synthetaseUniRule annotation
Short name:
AspRSUniRule annotation
Gene namesi
Name:aspSUniRule annotation
Synonyms:tls
Ordered Locus Names:b1866, JW1855
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10097. aspS.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 590590Aspartate--tRNA ligasePRO_0000110868Add
BLAST

Proteomic databases

EPDiP21889.
PaxDbiP21889.
PRIDEiP21889.

2D gel databases

SWISS-2DPAGEP21889.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4259330. 10 interactions.
DIPiDIP-9182N.
IntActiP21889. 26 interactions.
MINTiMINT-1249167.
STRINGi511145.b1866.

Chemistry

BindingDBiP21889.

Structurei

Secondary structure

1
590
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Helixi11 – 133Combined sources
Beta strandi17 – 2913Combined sources
Beta strandi34 – 407Combined sources
Beta strandi43 – 497Combined sources
Helixi51 – 533Combined sources
Helixi54 – 607Combined sources
Beta strandi68 – 7710Combined sources
Turni80 – 823Combined sources
Turni88 – 914Combined sources
Beta strandi92 – 10312Combined sources
Beta strandi112 – 1143Combined sources
Helixi118 – 1236Combined sources
Helixi125 – 1284Combined sources
Helixi132 – 15423Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi170 – 1734Combined sources
Beta strandi177 – 1793Combined sources
Beta strandi181 – 1833Combined sources
Beta strandi187 – 1893Combined sources
Helixi195 – 2039Combined sources
Beta strandi208 – 2169Combined sources
Beta strandi227 – 23812Combined sources
Helixi241 – 26020Combined sources
Beta strandi269 – 2713Combined sources
Helixi272 – 2798Combined sources
Beta strandi280 – 2834Combined sources
Beta strandi292 – 2943Combined sources
Helixi296 – 2994Combined sources
Helixi305 – 3128Combined sources
Beta strandi316 – 3238Combined sources
Helixi326 – 3283Combined sources
Helixi331 – 34313Combined sources
Beta strandi351 – 3555Combined sources
Helixi357 – 3637Combined sources
Helixi369 – 3713Combined sources
Helixi374 – 38310Combined sources
Beta strandi391 – 3988Combined sources
Helixi399 – 41618Combined sources
Beta strandi427 – 4315Combined sources
Beta strandi434 – 4385Combined sources
Beta strandi440 – 4423Combined sources
Beta strandi444 – 4485Combined sources
Beta strandi454 – 4563Combined sources
Helixi459 – 4646Combined sources
Turni466 – 4683Combined sources
Beta strandi470 – 4789Combined sources
Beta strandi481 – 4899Combined sources
Helixi493 – 50210Combined sources
Helixi507 – 52014Combined sources
Turni521 – 5244Combined sources
Beta strandi528 – 5347Combined sources
Helixi535 – 5439Combined sources
Helixi548 – 5514Combined sources
Beta strandi552 – 5543Combined sources
Turni563 – 5664Combined sources
Beta strandi567 – 5704Combined sources
Helixi573 – 5786Combined sources
Beta strandi581 – 5833Combined sources
Beta strandi586 – 5883Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C0AX-ray2.40A1-585[»]
1EQRX-ray2.70A/B/C1-590[»]
1IL2X-ray2.60A/B1-590[»]
ProteinModelPortaliP21889.
SMRiP21889. Positions 1-585.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21889.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni195 – 1984AspartateUniRule annotation

Sequence similaritiesi

Belongs to the class-II aminoacyl-tRNA synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C9M. Bacteria.
COG0173. LUCA.
HOGENOMiHOG000275159.
InParanoidiP21889.
KOiK01876.
OMAiYQLDVEM.
OrthoDBiEOG68Q0NX.
PhylomeDBiP21889.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.30.1360.30. 1 hit.
HAMAPiMF_00044. Asp_tRNA_synth.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004524. Asp-tRNA-ligase_bac/mit.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR004115. GAD-like.
IPR029351. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 2 hits.
PTHR22594:SF5. PTHR22594:SF5. 2 hits.
PfamiPF02938. GAD. 1 hit.
PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSiPR01042. TRNASYNTHASP.
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF55261. SSF55261. 1 hit.
TIGRFAMsiTIGR00459. aspS_bact. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P21889-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTEYCGQLR LSHVGQQVTL CGWVNRRRDL GSLIFIDMRD REGIVQVFFD
60 70 80 90 100
PDRADALKLA SELRNEFCIQ VTGTVRARDE KNINRDMATG EIEVLASSLT
110 120 130 140 150
IINRADVLPL DSNHVNTEEA RLKYRYLDLR RPEMAQRLKT RAKITSLVRR
160 170 180 190 200
FMDDHGFLDI ETPMLTKATP EGARDYLVPS RVHKGKFYAL PQSPQLFKQL
210 220 230 240 250
LMMSGFDRYY QIVKCFRDED LRADRQPEFT QIDVETSFMT APQVREVMEA
260 270 280 290 300
LVRHLWLEVK GVDLGDFPVM TFAEAERRYG SDKPDLRNPM ELTDVADLLK
310 320 330 340 350
SVEFAVFAGP ANDPKGRVAA LRVPGGASLT RKQIDEYGNF VKIYGAKGLA
360 370 380 390 400
YIKVNERAKG LEGINSPVAK FLNAEIIEDI LDRTAAQDGD MIFFGADNKK
410 420 430 440 450
IVADAMGALR LKVGKDLGLT DESKWAPLWV IDFPMFEDDG EGGLTAMHHP
460 470 480 490 500
FTSPKDMTAA ELKAAPENAV ANAYDMVING YEVGGGSVRI HNGDMQQTVF
510 520 530 540 550
GILGINEEEQ REKFGFLLDA LKYGTPPHAG LAFGLDRLTM LLTGTDNIRD
560 570 580 590
VIAFPKTTAA ACLMTEAPSF ANPTALAELS IQVVKKAENN
Length:590
Mass (Da):65,913
Last modified:May 1, 1991 - v1
Checksum:iA411D3E16D3A9284
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53863 Genomic DNA. Translation: CAA37856.1.
U00096 Genomic DNA. Translation: AAC74936.1.
AP009048 Genomic DNA. Translation: BAA15677.1.
X53984 Genomic DNA. Translation: CAA37932.1.
D10165 Genomic DNA. No translation available.
PIRiJT0942. SYECD.
RefSeqiNP_416380.1. NC_000913.3.
WP_001258678.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74936; AAC74936; b1866.
BAA15677; BAA15677; BAA15677.
GeneIDi946385.
KEGGiecj:JW1855.
eco:b1866.
PATRICi32119055. VBIEscCol129921_1945.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53863 Genomic DNA. Translation: CAA37856.1.
U00096 Genomic DNA. Translation: AAC74936.1.
AP009048 Genomic DNA. Translation: BAA15677.1.
X53984 Genomic DNA. Translation: CAA37932.1.
D10165 Genomic DNA. No translation available.
PIRiJT0942. SYECD.
RefSeqiNP_416380.1. NC_000913.3.
WP_001258678.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C0AX-ray2.40A1-585[»]
1EQRX-ray2.70A/B/C1-590[»]
1IL2X-ray2.60A/B1-590[»]
ProteinModelPortaliP21889.
SMRiP21889. Positions 1-585.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259330. 10 interactions.
DIPiDIP-9182N.
IntActiP21889. 26 interactions.
MINTiMINT-1249167.
STRINGi511145.b1866.

Chemistry

BindingDBiP21889.

2D gel databases

SWISS-2DPAGEP21889.

Proteomic databases

EPDiP21889.
PaxDbiP21889.
PRIDEiP21889.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74936; AAC74936; b1866.
BAA15677; BAA15677; BAA15677.
GeneIDi946385.
KEGGiecj:JW1855.
eco:b1866.
PATRICi32119055. VBIEscCol129921_1945.

Organism-specific databases

EchoBASEiEB0095.
EcoGeneiEG10097. aspS.

Phylogenomic databases

eggNOGiENOG4105C9M. Bacteria.
COG0173. LUCA.
HOGENOMiHOG000275159.
InParanoidiP21889.
KOiK01876.
OMAiYQLDVEM.
OrthoDBiEOG68Q0NX.
PhylomeDBiP21889.

Enzyme and pathway databases

BioCyciEcoCyc:ASPS-MONOMER.
ECOL316407:JW1855-MONOMER.
MetaCyc:ASPS-MONOMER.
BRENDAi6.1.1.12. 2026.
SABIO-RKP21889.

Miscellaneous databases

EvolutionaryTraceiP21889.
PROiP21889.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.30.1360.30. 1 hit.
HAMAPiMF_00044. Asp_tRNA_synth.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004524. Asp-tRNA-ligase_bac/mit.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR004115. GAD-like.
IPR029351. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 2 hits.
PTHR22594:SF5. PTHR22594:SF5. 2 hits.
PfamiPF02938. GAD. 1 hit.
PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSiPR01042. TRNASYNTHASP.
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF55261. SSF55261. 1 hit.
TIGRFAMsiTIGR00459. aspS_bact. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Aspartyl-tRNA synthetase from Escherichia coli: cloning and characterisation of the gene, homologies of its translated amino acid sequence with asparaginyl- and lysyl-tRNA synthetases."
    Eriani G., Dirheimer G., Gangloff J.
    Nucleic Acids Res. 18:7109-7118(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  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. "Location of a mutation in the aspartyl-tRNA synthetase gene of Escherichia coli K12."
    Sharples G.J., Lloyd R.G.
    Mutat. Res. 264:93-96(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 382-590.
    Strain: K12.
  6. "Molecular analysis of the Escherichia coli ruvC gene, which encodes a Holliday junction-specific endonuclease."
    Takahagi M., Iwasaki H., Nakata A., Shinagawa H.
    J. Bacteriol. 173:5747-5753(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 461-590.
  7. "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.
  8. "Synthesis of aspartyl-tRNA(Asp) in Escherichia coli - a snapshot of the second step."
    Eiler S., Dock-Bregeon A.-C., Moulinier L., Thierry J.-C., Moras D.
    EMBO J. 18:6532-6541(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  9. "Aspartyl tRNA-synthetase from Escherichia coli: flexibility and adaptability to the substrates."
    Rees B., Webster G., Delarue M., Boeglin M., Moras D.
    J. Mol. Biol. 299:1157-1164(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).

Entry informationi

Entry nameiSYD_ECOLI
AccessioniPrimary (citable) accession number: P21889
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: March 16, 2016
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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.