SYE_THET8
ID SYE_THET8 Reviewed; 468 AA.
AC P27000; Q5SL55;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Glutamate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00022};
DE EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022};
DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00022};
DE Short=GluRS {ECO:0000255|HAMAP-Rule:MF_00022};
GN Name=gltX {ECO:0000255|HAMAP-Rule:MF_00022}; OrderedLocusNames=TTHA0438;
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].
RX PubMed=1541262; DOI=10.1111/j.1432-1033.1992.tb16656.x;
RA Nureki O., Suzuki K., Hara-Yokoyama M., Kohno T., Matsuzawa H., Ohta T.,
RA Shimizu T., Morikawa K., Miyazawa T., Yokoyama S.;
RT "Glutamyl-tRNA synthetase from Thermus thermophilus HB8. Molecular cloning
RT of the gltX gene and crystallization of the overproduced protein.";
RL Eur. J. Biochem. 204:465-472(1992).
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 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=7701318; DOI=10.1126/science.7701318;
RA Nureki O., Vassylyev D.G., Katayanagi K., Shimizu T., Sekine S., Kigawa T.,
RA Miyazawa T., Yokoyama S., Morikawa K.;
RT "Architectures of class-defining and specific domains of glutamyl-tRNA
RT synthetase.";
RL Science 267:1958-1965(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH TRNA-GLU, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-358.
RX PubMed=11224561; DOI=10.1038/84927;
RA Sekine S., Nureki O., Shimada A., Vassylyev D.G., Yokoyama S.;
RT "Structural basis for anticodon recognition by discriminating glutamyl-tRNA
RT synthetase.";
RL Nat. Struct. Biol. 8:203-206(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH ATP; GLUTAMATE AND
RP TRNA.
RX PubMed=12554668; DOI=10.1093/emboj/cdg053;
RA Sekine S., Nureki O., Dubois D.Y., Bernier S., Chenevert R., Lapointe J.,
RA Vassylyev D.G., Yokoyama S.;
RT "ATP binding by glutamyl-tRNA synthetase is switched to the productive mode
RT by tRNA binding.";
RL EMBO J. 22:676-688(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH ATP; GLUTAMATE AND
RP TRNA, FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=17161369; DOI=10.1016/j.str.2006.10.005;
RA Sekine S., Shichiri M., Bernier S., Chenevert R., Lapointe J., Yokoyama S.;
RT "Structural bases of transfer RNA-dependent amino acid recognition and
RT activation by glutamyl-tRNA synthetase.";
RL Structure 14:1791-1799(2006).
CC -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-
CC step reaction: glutamate is first activated by ATP to form Glu-AMP and
CC then transferred to the acceptor end of tRNA(Glu). {ECO:0000255|HAMAP-
CC Rule:MF_00022, ECO:0000269|PubMed:11224561,
CC ECO:0000269|PubMed:17161369}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663,
CC Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC ChEBI:CHEBI:456215; EC=6.1.1.17; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00022};
CC -!- ACTIVITY REGULATION: In the absence of bound tRNA, ATP is bound in a
CC non-productive mode, and the enzyme cannot activate amino acids.
CC {ECO:0000269|PubMed:17161369}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.7 uM for tRNA-Glu {ECO:0000269|PubMed:11224561};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00022,
CC ECO:0000269|PubMed:11224561}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00022}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 1 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00022}.
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DR EMBL; X64557; CAA45854.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70261.1; -; Genomic_DNA.
DR RefSeq; WP_011227935.1; NC_006461.1.
DR RefSeq; YP_143704.1; NC_006461.1.
DR PDB; 1G59; X-ray; 2.40 A; A/C=1-468.
DR PDB; 1GLN; X-ray; 2.50 A; A=1-468.
DR PDB; 1J09; X-ray; 1.80 A; A=1-468.
DR PDB; 1N75; X-ray; 1.90 A; A=1-468.
DR PDB; 1N77; X-ray; 2.40 A; A/B=1-468.
DR PDB; 1N78; X-ray; 2.10 A; A/B=1-468.
DR PDB; 2CUZ; X-ray; 1.98 A; A=1-468.
DR PDB; 2CV0; X-ray; 2.40 A; A/B=1-468.
DR PDB; 2CV1; X-ray; 2.41 A; A/B=1-468.
DR PDB; 2CV2; X-ray; 2.69 A; A/B=1-468.
DR PDB; 2DXI; X-ray; 2.20 A; A/B=1-468.
DR PDBsum; 1G59; -.
DR PDBsum; 1GLN; -.
DR PDBsum; 1J09; -.
DR PDBsum; 1N75; -.
DR PDBsum; 1N77; -.
DR PDBsum; 1N78; -.
DR PDBsum; 2CUZ; -.
DR PDBsum; 2CV0; -.
DR PDBsum; 2CV1; -.
DR PDBsum; 2CV2; -.
DR PDBsum; 2DXI; -.
DR AlphaFoldDB; P27000; -.
DR SMR; P27000; -.
DR DIP; DIP-29168N; -.
DR STRING; 300852.55771820; -.
DR EnsemblBacteria; BAD70261; BAD70261; BAD70261.
DR GeneID; 3168748; -.
DR KEGG; ttj:TTHA0438; -.
DR PATRIC; fig|300852.9.peg.438; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_015768_6_3_0; -.
DR OMA; WDEGPFF; -.
DR PhylomeDB; P27000; -.
DR BRENDA; 6.1.1.17; 2305.
DR SABIO-RK; P27000; -.
DR EvolutionaryTrace; P27000; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00808; GluRS_core; 1.
DR Gene3D; 1.10.10.350; -; 1.
DR Gene3D; 1.10.8.70; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00022; Glu_tRNA_synth_type1; 1.
DR InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR InterPro; IPR020752; Glu-tRNA-synth_I_codon-bd_sub1.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR033910; GluRS_core.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF19269; Anticodon_2; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF48163; SSF48163; 1.
DR TIGRFAMs; TIGR00464; gltX_bact; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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..468
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000119683"
FT REGION 432..447
FT /note="Interaction with tRNA"
FT MOTIF 8..18
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT MOTIF 243..247
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 5..7
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 41
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 187..191
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 205
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 243..247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT SITE 354
FT /note="Interaction with tRNA; via carbonyl oxygen"
FT SITE 358
FT /note="Essential for discrimination between tRNA(Glu) and
FT tRNA(Gln)"
FT MUTAGEN 358
FT /note="R->Q: Reduces affinity for tRNA and abolishes the
FT ability to discriminate between tRNA(Glu) and tRNA(Gln)."
FT /evidence="ECO:0000269|PubMed:11224561"
FT CONFLICT 74..77
FT /note="GGPH -> AAPT (in Ref. 1; CAA45854)"
FT /evidence="ECO:0000305"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1J09"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 16..31
FT /evidence="ECO:0007829|PDB:1J09"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1J09"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:1N75"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:1J09"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1J09"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1J09"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1G59"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:1J09"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:1J09"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1J09"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:1J09"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:1J09"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:1J09"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:1J09"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:1J09"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1J09"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2CUZ"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 253..258
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 263..273
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 286..292
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 307..320
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 324..337
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 345..355
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 364..368
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 381..403
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 409..423
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 427..439
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 447..453
FT /evidence="ECO:0007829|PDB:1J09"
FT HELIX 456..467
FT /evidence="ECO:0007829|PDB:1J09"
SQ SEQUENCE 468 AA; 53910 MW; 920E7F3363AF19E9 CRC64;
MVVTRIAPSP TGDPHVGTAY IALFNYAWAR RNGGRFIVRI EDTDRARYVP GAEERILAAL
KWLGLSYDEG PDVGGPHGPY RQSERLPLYQ KYAEELLKRG WAYRAFETPE ELEQIRKEKG
GYDGRARNIP PEEAEERARR GEPHVIRLKV PRPGTTEVKD ELRGVVVYDN QEIPDVVLLK
SDGYPTYHLA NVVDDHLMGV TDVIRAEEWL VSTPIHVLLY RAFGWEAPRF YHMPLLRNPD
KTKISKRKSH TSLDWYKAEG FLPEALRNYL CLMGFSMPDG REIFTLEEFI QAFTWERVSL
GGPVFDLEKL RWMNGKYIRE VLSLEEVAER VKPFLREAGL SWESEAYLRR AVELMRPRFD
TLKEFPEKAR YLFTEDYPVS EKAQRKLEEG LPLLKELYPR LRAQEEWTEA ALEALLRGFA
AEKGVKLGQV AQPLRAALTG SLETPGLFEI LALLGKERAL RRLERALA
