SYE_BORBU
ID SYE_BORBU Reviewed; 490 AA.
AC O51345;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=BB_0372;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
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; AE000783; AAC66742.1; -; Genomic_DNA.
DR PIR; C70146; C70146.
DR RefSeq; NP_212506.1; NC_001318.1.
DR RefSeq; WP_002665196.1; NC_001318.1.
DR PDB; 4GRI; X-ray; 2.60 A; A/B=2-490.
DR PDBsum; 4GRI; -.
DR AlphaFoldDB; O51345; -.
DR SMR; O51345; -.
DR STRING; 224326.BB_0372; -.
DR PRIDE; O51345; -.
DR EnsemblBacteria; AAC66742; AAC66742; BB_0372.
DR KEGG; bbu:BB_0372; -.
DR PATRIC; fig|224326.49.peg.767; -.
DR HOGENOM; CLU_015768_6_3_12; -.
DR OMA; WDEGPFF; -.
DR Proteomes; UP000001807; 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; 1.10.1160.10; -; 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; 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; IPR020061; Glu_tRNA_lig_a-bdl.
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.
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..490
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000119517"
FT MOTIF 9..19
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT MOTIF 251..255
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:4GRI"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 17..32
FT /evidence="ECO:0007829|PDB:4GRI"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:4GRI"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4GRI"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:4GRI"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 110..122
FT /evidence="ECO:0007829|PDB:4GRI"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:4GRI"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:4GRI"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:4GRI"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:4GRI"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:4GRI"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 195..205
FT /evidence="ECO:0007829|PDB:4GRI"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:4GRI"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:4GRI"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:4GRI"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 271..280
FT /evidence="ECO:0007829|PDB:4GRI"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:4GRI"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 315..328
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 331..344
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 354..368
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 376..380
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:4GRI"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 405..417
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 425..438
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 444..454
FT /evidence="ECO:0007829|PDB:4GRI"
FT STRAND 455..459
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 463..470
FT /evidence="ECO:0007829|PDB:4GRI"
FT HELIX 472..486
FT /evidence="ECO:0007829|PDB:4GRI"
SQ SEQUENCE 490 AA; 56752 MW; E7ED6AD2474934F4 CRC64;
MSTRVRYAPS PTGLQHIGGI RTALFNYFFA KSCGGKFLLR IEDTDQSRYS PEAENDLYSS
LKWLGISFDE GPVVGGDYAP YVQSQRSAIY KQYAKYLIES GHAYYCYCSP ERLERIKKIQ
NINKMPPGYD RHCRNLSNEE VENALIKKIK PVVRFKIPLE GDTSFDDILL GRITWANKDI
SPDPVILKSD GLPTYHLANV VDDYLMKITH VLRAQEWVSS GPLHVLLYKA FKWKPPIYCH
LPMVMGNDGQ KLSKRHGSTA LRQFIEDGYL PEAIINYVTL LGWSYDDKRE FFSKNDLEQF
FSIEKINKSP AIFDYHKLDF FNSYYIREKK DEDLFNLLLP FFQKKGYVSK PSTLEENQKL
KLLIPLIKSR IKKLSDALNM TKFFYEDIKS WNLDEFLSRK KTAKEVCSIL ELIKPILEGF
EKRSSEENDK IFYDFAESNG FKLGEILLPI RIAALGSKVS PPLFDSLKLI GKSKVFERIK
LAQEFLRINE
