SYE_BURTA
ID SYE_BURTA Reviewed; 469 AA.
AC Q2SX36;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=BTH_I1984;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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}.
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 -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00022}.
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; CP000086; ABC37833.1; -; Genomic_DNA.
DR RefSeq; WP_009890362.1; NZ_CP008785.1.
DR PDB; 4G6Z; X-ray; 2.05 A; A=1-469.
DR PDBsum; 4G6Z; -.
DR AlphaFoldDB; Q2SX36; -.
DR SMR; Q2SX36; -.
DR PRIDE; Q2SX36; -.
DR EnsemblBacteria; ABC37833; ABC37833; BTH_I1984.
DR GeneID; 66547525; -.
DR KEGG; bte:BTH_I1984; -.
DR HOGENOM; CLU_015768_6_0_4; -.
DR OMA; WDEGPFF; -.
DR OrthoDB; 1409413at2; -.
DR Proteomes; UP000001930; Chromosome I.
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; 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; 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.
FT CHAIN 1..469
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000237349"
FT REGION 118..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 11..21
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 246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 19..34
FT /evidence="ECO:0007829|PDB:4G6Z"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:4G6Z"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:4G6Z"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:4G6Z"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:4G6Z"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:4G6Z"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:4G6Z"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:4G6Z"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:4G6Z"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:4G6Z"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:4G6Z"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:4G6Z"
FT TURN 246..249
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 253..258
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:4G6Z"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 285..291
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 306..319
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 322..334
FT /evidence="ECO:0007829|PDB:4G6Z"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 340..345
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 349..356
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 363..370
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 448..454
FT /evidence="ECO:0007829|PDB:4G6Z"
FT HELIX 457..465
FT /evidence="ECO:0007829|PDB:4G6Z"
SQ SEQUENCE 469 AA; 52046 MW; EEE0D68248D730E0 CRC64;
MTRPVRTRFA PSPTGFIHLG NIRSALYPWA FARKMKGTFV LRIEDTDVER SSQEAVDAIL
EGMAWLGLDY DEGPYYQMQR MDRYREVLAQ MQEKGLVYPC YMSTEELDAL RERQRAAGEK
PRYDGTWRPE PGKVLPEPPA GVAPVLRFRN PLTGTVAWDD AVKGRVEISN EELDDLVVAR
PDGTPMYNFC VVVDDLDMGI THVIRGDDHV NNTPRQINIL RALGGEVPVY AHLPTVLNEQ
GEKMSKRHGA MSVMGYRDAG YLPEAVLNYL ARLGWSHGDA EIFTREQFVE WFDLEHLGKS
PAQYDHNKLN WLNNHYIKEA DDARLAGLAK PFFAALGIDA GAIEQGPDLV SVMGLMKDRA
STVKEIAENS AMFYRAPAPG ADALAQHVTD AVRPALVEFA AALKTVEWTK EAIAAALKAV
LGAHKLKMPQ LAMPVRLLVA GTTHTPSIDA VLLLFGRDVV VSRIEAALA
