SYD_THETH
ID SYD_THETH Reviewed; 580 AA.
AC P36419;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Aspartate--tRNA(Asp) ligase;
DE EC=6.1.1.12;
DE AltName: Full=Aspartyl-tRNA synthetase;
DE Short=AspRS;
DE AltName: Full=Discriminating aspartyl-tRNA synthetase;
DE Short=D-AspRS;
GN Name=aspS;
OS Thermus thermophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=VK1;
RX PubMed=8319804; DOI=10.1016/0014-5793(93)81069-c;
RA Poterszman A., Plateau P., Moras D., Blanquet S., Mazuric M.-H.,
RA Kreutzer R., Kern D.;
RT "Sequence, overproduction and crystallization of aspartyl-tRNA synthetase
RT from Thermus thermophilus. Implications for the structure of prokaryotic
RT aspartyl-tRNA synthetases.";
RL FEBS Lett. 325:183-186(1993).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=8045252; DOI=10.1002/j.1460-2075.1994.tb06623.x;
RA Delarue M., Poterszman A., Nikonov S., Garber M., Moras D., Thierry J.-C.;
RT "Crystal structure of a prokaryotic aspartyl tRNA-synthetase.";
RL EMBO J. 13:3219-3229(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH AMP AND
RP ASPARTYL-AMP.
RX PubMed=7966328; DOI=10.1006/jmbi.1994.1716;
RA Poterszman A., Delarue M., Thierry J.C., Moras D.;
RT "Synthesis and recognition of aspartyl-adenylate by Thermus thermophilus
RT aspartyl-tRNA synthetase.";
RL J. Mol. Biol. 244:158-167(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH TRNA(ASP).
RX PubMed=10843857; DOI=10.1006/jmbi.2000.3819;
RA Briand C., Poterszman A., Eiler S., Webster G., Thierry J.-C., Moras D.;
RT "An intermediate step in the recognition of tRNA(Asp) by aspartyl-tRNA
RT synthetase.";
RL J. Mol. Biol. 299:1051-1060(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS).
RX PubMed=11914489; DOI=10.1107/s0907444902003177;
RA Ng J.D., Sauter C., Lorber B., Kirkland N., Arnez J., Giege R.;
RT "Comparative analysis of space-grown and earth-grown crystals of an
RT aminoacyl-tRNA synthetase: space-grown crystals are more useful for
RT structural determination.";
RL Acta Crystallogr. D 58:645-652(2002).
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).
CC {ECO:0000255|HAMAP-Rule:MF_00044}.
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};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00044,
CC ECO:0000269|PubMed:10843857, ECO:0000269|PubMed:7966328}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00044}.
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; X70943; CAA50282.1; -; Genomic_DNA.
DR RefSeq; WP_011172809.1; NZ_CP053287.1.
DR PDB; 1EFW; X-ray; 3.00 A; A/B=1-580.
DR PDB; 1G51; X-ray; 2.40 A; A/B=1-580.
DR PDB; 1L0W; X-ray; 2.01 A; A/B=1-580.
DR PDBsum; 1EFW; -.
DR PDBsum; 1G51; -.
DR PDBsum; 1L0W; -.
DR AlphaFoldDB; P36419; -.
DR SMR; P36419; -.
DR DrugBank; DB01895; Aspartyl-Adenosine-5'-Monophosphate.
DR GeneID; 3169335; -.
DR BRENDA; 6.1.1.12; 2305.
DR SABIO-RK; P36419; -.
DR EvolutionaryTrace; P36419; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
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;
KW Direct protein sequencing; Ligase; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..580
FT /note="Aspartate--tRNA(Asp) ligase"
FT /id="PRO_0000110971"
FT REGION 201..204
FT /note="Aspartate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 177
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 223..225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 223
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 442
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 476
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 483
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 528..531
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 18..30
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1G51"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 68..77
FT /evidence="ECO:0007829|PDB:1L0W"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 90..101
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 138..160
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 213..222
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 233..244
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 247..265
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 279..286
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 317..327
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 331..343
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 350..355
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 371..378
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 385..392
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 393..410
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:1L0W"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:1L0W"
FT TURN 451..454
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 455..458
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 464..472
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 475..483
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 487..497
FT /evidence="ECO:0007829|PDB:1L0W"
FT TURN 501..503
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 504..507
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 509..514
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 522..528
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 529..537
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 542..545
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:1L0W"
FT TURN 557..560
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 561..564
FT /evidence="ECO:0007829|PDB:1L0W"
FT HELIX 567..572
FT /evidence="ECO:0007829|PDB:1L0W"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:1L0W"
SQ SEQUENCE 580 AA; 66030 MW; 510C79B25CF95D4E CRC64;
MRRTHYAGSL RETHVGEEVV LEGWVNRRRD LGGLIFLDLR DREGLVQLVA HPASPAYATA
ERVRPEWVVR AKGLVRLRPE PNPRLATGRV EVELSALEVL AEAKTPPFPV DAGWRGEEEK
EASEELRLKY RYLDLRRRRM QENLRLRHRV IKAIWDFLDR EGFVQVETPF LTKSTPEGAR
DFLVPYRHEP GLFYALPQSP QLFKQMLMVA GLDRYFQIAR CFRDEDLRAD RQPDFTQLDL
EMSFVEVEDV LELNERLMAH VFREALGVEL PLPFPRLSYE EAMERYGSDK PDLRFGLELK
EVGPLFRQSG FRVFQEAESV KALALPKALS RKEVAELEEV AKRHKAQGLA WARVEEGGFS
GGVAKFLEPV REALLQATEA RPGDTLLFVA GPRKVAATAL GAVRLRAADL LGLKREGFRF
LWVVDFPLLE WDEEEEAWTY MHHPFTSPHP EDLPLLEKDP GRVRALAYDL VLNGVEVGGG
SIRIHDPRLQ ARVFRLLGIG EEEQREKFGF FLEALEYGAP PHGGIAWGLD RLLALMTGSP
SIREVIAFPK NKEGKDPLTG APSPVPEEQL RELGLMVVRP
