SYD_THET8
ID SYD_THET8 Reviewed; 580 AA.
AC Q5SKD2;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Aspartate--tRNA(Asp) ligase;
DE EC=6.1.1.12;
DE AltName: Full=Aspartyl-tRNA synthetase 1;
DE Short=AspRS1;
DE AltName: Full=Discriminating aspartyl-tRNA synthetase;
DE Short=D-AspRS;
GN Name=aspS1; OrderedLocusNames=TTHA0711;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 1-52; 209-230 AND 259-283, FUNCTION, CATALYTIC
RP ACTIVITY, KINETIC PARAMETERS, SUBUNIT, AND INDUCTION.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=9220965; DOI=10.1021/bi970392v;
RA Becker H.D., Reinbolt J., Kreutzer R., Giege R., Kern D.;
RT "Existence of two distinct aspartyl-tRNA synthetases in Thermus
RT thermophilus. Structural and biochemical properties of the two enzymes.";
RL Biochemistry 36:8785-8797(1997).
RN [4]
RP GENE NAME, FUNCTION AS A DISCRIMINATING ASPRS, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, AND KINETIC PARAMETERS.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=10727213; DOI=10.1021/bi992573y;
RA Becker H.D., Roy H., Moulinier L., Mazauric M.H., Keith G., Kern D.;
RT "Thermus thermophilus contains an eubacterial and an archaebacterial
RT aspartyl-tRNA synthetase.";
RL Biochemistry 39:3216-3230(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). Is specific
CC for tRNA(Asp) since it aspartylates tRNA(Asn) 3 orders of magnitude
CC less efficiently than tRNA(Asp). {ECO:0000269|PubMed:10727213,
CC ECO:0000269|PubMed:9220965}.
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:10727213,
CC ECO:0000269|PubMed:9220965};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9 uM for L-aspartate (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:10727213, ECO:0000269|PubMed:9220965};
CC KM=30 uM for L-aspartate (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:10727213, ECO:0000269|PubMed:9220965};
CC KM=120 uM for ATP (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:10727213, ECO:0000269|PubMed:9220965};
CC KM=280 uM for ATP (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:10727213, ECO:0000269|PubMed:9220965};
CC KM=0.044 uM for tRNA(Asp) (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:10727213, ECO:0000269|PubMed:9220965};
CC KM=0.030 uM for tRNA(Asp) (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:10727213, ECO:0000269|PubMed:9220965};
CC KM=3.4 uM for tRNA(Asn) (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:10727213, ECO:0000269|PubMed:9220965};
CC Note=kcat is 0.77 sec(-1) for tRNA(Asp) aspartylation at 37 degrees
CC Celsius and 2.7 sec(-1) at 70 degrees Celsius. kcat is 0.12 sec(-1)
CC for tRNA(Asn) aspartylation at 70 degrees Celsius.;
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00044,
CC ECO:0000269|PubMed:9220965}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00044}.
CC -!- INDUCTION: Constitutively expressed in a constant ratio along the
CC growth of the bacterium. {ECO:0000269|PubMed:9220965}.
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; AP008226; BAD70534.1; -; Genomic_DNA.
DR RefSeq; WP_011172809.1; NC_006461.1.
DR RefSeq; YP_143977.1; NC_006461.1.
DR PDB; 6HHV; X-ray; 2.18 A; A/B=1-580.
DR PDB; 6HHW; X-ray; 2.20 A; A/B=1-580.
DR PDB; 6HHX; X-ray; 2.10 A; A/B=1-580.
DR PDB; 6SJC; X-ray; 2.23 A; A/B=1-580.
DR PDB; 7AP4; X-ray; 2.15 A; A/B=1-580.
DR PDBsum; 6HHV; -.
DR PDBsum; 6HHW; -.
DR PDBsum; 6HHX; -.
DR PDBsum; 6SJC; -.
DR PDBsum; 7AP4; -.
DR AlphaFoldDB; Q5SKD2; -.
DR SMR; Q5SKD2; -.
DR STRING; 300852.55772093; -.
DR EnsemblBacteria; BAD70534; BAD70534; BAD70534.
DR GeneID; 3169335; -.
DR KEGG; ttj:TTHA0711; -.
DR PATRIC; fig|300852.9.peg.705; -.
DR eggNOG; COG0173; Bacteria.
DR HOGENOM; CLU_014330_3_2_0; -.
DR OMA; YQLDVEM; -.
DR PhylomeDB; Q5SKD2; -.
DR Proteomes; UP000000532; Chromosome.
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; Reference proteome.
FT CHAIN 1..580
FT /note="Aspartate--tRNA(Asp) ligase"
FT /id="PRO_0000110970"
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:6HHX"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 18..31
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 68..77
FT /evidence="ECO:0007829|PDB:6HHX"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 90..101
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 138..160
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:6HHX"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 233..244
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 247..266
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 279..286
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 318..327
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 331..343
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 350..354
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 371..378
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 385..392
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 393..410
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 427..430
FT /evidence="ECO:0007829|PDB:6HHX"
FT TURN 433..436
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 450..454
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 455..458
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 464..472
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 475..483
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 487..497
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 501..514
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 522..528
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 529..537
FT /evidence="ECO:0007829|PDB:6HHX"
FT HELIX 542..545
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:6HHX"
FT TURN 557..559
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:7AP4"
FT HELIX 567..571
FT /evidence="ECO:0007829|PDB:6HHX"
FT TURN 572..574
FT /evidence="ECO:0007829|PDB:6HHX"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:6HHX"
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
