SYD_ECOLI
ID SYD_ECOLI Reviewed; 590 AA.
AC P21889;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Aspartate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00044};
DE EC=6.1.1.12 {ECO:0000255|HAMAP-Rule:MF_00044, ECO:0000269|PubMed:10918062};
DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044};
DE Short=AspRS {ECO:0000255|HAMAP-Rule:MF_00044};
GN Name=aspS {ECO:0000255|HAMAP-Rule:MF_00044}; Synonyms=tls;
GN OrderedLocusNames=b1866, JW1855;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2129559; DOI=10.1093/nar/18.23.7109;
RA Eriani G., Dirheimer G., Gangloff J.;
RT "Aspartyl-tRNA synthetase from Escherichia coli: cloning and
RT characterisation of the gene, homologies of its translated amino acid
RT sequence with asparaginyl- and lysyl-tRNA synthetases.";
RL Nucleic Acids Res. 18:7109-7118(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 382-590.
RC STRAIN=K12;
RX PubMed=1944398; DOI=10.1016/0165-7992(91)90122-k;
RA Sharples G.J., Lloyd R.G.;
RT "Location of a mutation in the aspartyl-tRNA synthetase gene of Escherichia
RT coli K12.";
RL Mutat. Res. 264:93-96(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 461-590.
RX PubMed=1885548; DOI=10.1128/jb.173.18.5747-5753.1991;
RA Takahagi M., Iwasaki H., Nakata A., Shinagawa H.;
RT "Molecular analysis of the Escherichia coli ruvC gene, which encodes a
RT Holliday junction-specific endonuclease.";
RL J. Bacteriol. 173:5747-5753(1991).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=K12 / K37;
RX PubMed=10918062; DOI=10.1074/jbc.m005166200;
RA Soutourina J., Plateau P., Blanquet S.;
RT "Metabolism of D-aminoacyl-tRNAs in Escherichia coli and Saccharomyces
RT cerevisiae cells.";
RL J. Biol. Chem. 275:32535-32542(2000).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=10562565; DOI=10.1093/emboj/18.22.6532;
RA Eiler S., Dock-Bregeon A.-C., Moulinier L., Thierry J.-C., Moras D.;
RT "Synthesis of aspartyl-tRNA(Asp) in Escherichia coli - a snapshot of the
RT second step.";
RL EMBO J. 18:6532-6541(1999).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=10873442; DOI=10.1006/jmbi.2000.3792;
RA Rees B., Webster G., Delarue M., Boeglin M., Moras D.;
RT "Aspartyl tRNA-synthetase from Escherichia coli: flexibility and
RT adaptability to the substrates.";
RL J. Mol. Biol. 299:1157-1164(2000).
CC -!- FUNCTION: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a
CC two-step reaction: L-aspartate is first activated by ATP to form Asp-
CC AMP and then transferred to the acceptor end of tRNA(Asp). Also
CC mischarges tRNA(Asp) with D-aspartate, although it is a poor substrate
CC (PubMed:10918062). {ECO:0000255|HAMAP-Rule:MF_00044,
CC ECO:0000269|PubMed:10918062}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC ChEBI:CHEBI:456215; EC=6.1.1.12; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00044, ECO:0000269|PubMed:10918062};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00044}.
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DR EMBL; X53863; CAA37856.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74936.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15677.1; -; Genomic_DNA.
DR EMBL; X53984; CAA37932.1; -; Genomic_DNA.
DR EMBL; D10165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JT0942; SYECD.
DR RefSeq; NP_416380.1; NC_000913.3.
DR RefSeq; WP_001258678.1; NZ_SSZK01000001.1.
DR PDB; 1C0A; X-ray; 2.40 A; A=1-585.
DR PDB; 1EQR; X-ray; 2.70 A; A/B/C=1-590.
DR PDB; 1IL2; X-ray; 2.60 A; A/B=1-590.
DR PDBsum; 1C0A; -.
DR PDBsum; 1EQR; -.
DR PDBsum; 1IL2; -.
DR AlphaFoldDB; P21889; -.
DR SMR; P21889; -.
DR BioGRID; 4259330; 32.
DR DIP; DIP-9182N; -.
DR IntAct; P21889; 27.
DR STRING; 511145.b1866; -.
DR BindingDB; P21889; -.
DR ChEMBL; CHEMBL4295574; -.
DR SWISS-2DPAGE; P21889; -.
DR jPOST; P21889; -.
DR PaxDb; P21889; -.
DR PRIDE; P21889; -.
DR EnsemblBacteria; AAC74936; AAC74936; b1866.
DR EnsemblBacteria; BAA15677; BAA15677; BAA15677.
DR GeneID; 946385; -.
DR KEGG; ecj:JW1855; -.
DR KEGG; eco:b1866; -.
DR PATRIC; fig|1411691.4.peg.382; -.
DR EchoBASE; EB0095; -.
DR eggNOG; COG0173; Bacteria.
DR HOGENOM; CLU_014330_3_2_6; -.
DR InParanoid; P21889; -.
DR OMA; YQLDVEM; -.
DR PhylomeDB; P21889; -.
DR BioCyc; EcoCyc:ASPS-MON; -.
DR BioCyc; MetaCyc:ASPS-MON; -.
DR BRENDA; 6.1.1.12; 2026.
DR SABIO-RK; P21889; -.
DR EvolutionaryTrace; P21889; -.
DR PRO; PR:P21889; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IDA:EcoCyc.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1360.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00044; Asp_tRNA_synth_type1; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004524; Asp-tRNA-ligase_1.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR029351; GAD_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR PANTHER; PTHR22594:SF5; PTHR22594:SF5; 1.
DR Pfam; PF02938; GAD; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55261; SSF55261; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00459; aspS_bact; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..590
FT /note="Aspartate--tRNA ligase"
FT /id="PRO_0000110868"
FT REGION 195..198
FT /note="Aspartate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 171
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 217..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 217
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 448
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 482
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 489
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 534..537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 17..29
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 68..77
FT /evidence="ECO:0007829|PDB:1C0A"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1C0A"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 92..103
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1EQR"
FT HELIX 118..123
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 132..154
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 208..216
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 227..238
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 241..260
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 272..279
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:1EQR"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 305..312
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 316..323
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 331..343
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 357..363
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 374..383
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 391..398
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 399..416
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 427..431
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 434..438
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 444..448
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 459..464
FT /evidence="ECO:0007829|PDB:1C0A"
FT TURN 466..468
FT /evidence="ECO:0007829|PDB:1IL2"
FT STRAND 470..478
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 481..489
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 493..502
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 507..520
FT /evidence="ECO:0007829|PDB:1C0A"
FT TURN 521..524
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 528..534
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 535..543
FT /evidence="ECO:0007829|PDB:1C0A"
FT HELIX 548..551
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:1C0A"
FT TURN 563..566
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 567..570
FT /evidence="ECO:0007829|PDB:1IL2"
FT HELIX 573..578
FT /evidence="ECO:0007829|PDB:1C0A"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:1IL2"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:1EQR"
SQ SEQUENCE 590 AA; 65913 MW; A411D3E16D3A9284 CRC64;
MRTEYCGQLR LSHVGQQVTL CGWVNRRRDL GSLIFIDMRD REGIVQVFFD PDRADALKLA
SELRNEFCIQ VTGTVRARDE KNINRDMATG EIEVLASSLT IINRADVLPL DSNHVNTEEA
RLKYRYLDLR RPEMAQRLKT RAKITSLVRR FMDDHGFLDI ETPMLTKATP EGARDYLVPS
RVHKGKFYAL PQSPQLFKQL LMMSGFDRYY QIVKCFRDED LRADRQPEFT QIDVETSFMT
APQVREVMEA LVRHLWLEVK GVDLGDFPVM TFAEAERRYG SDKPDLRNPM ELTDVADLLK
SVEFAVFAGP ANDPKGRVAA LRVPGGASLT RKQIDEYGNF VKIYGAKGLA YIKVNERAKG
LEGINSPVAK FLNAEIIEDI LDRTAAQDGD MIFFGADNKK IVADAMGALR LKVGKDLGLT
DESKWAPLWV IDFPMFEDDG EGGLTAMHHP FTSPKDMTAA ELKAAPENAV ANAYDMVING
YEVGGGSVRI HNGDMQQTVF GILGINEEEQ REKFGFLLDA LKYGTPPHAG LAFGLDRLTM
LLTGTDNIRD VIAFPKTTAA ACLMTEAPSF ANPTALAELS IQVVKKAENN
