SYE_BACTN
ID SYE_BACTN Reviewed; 504 AA.
AC Q8A455;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=BT_2748;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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; AE015928; AAO77854.1; -; Genomic_DNA.
DR RefSeq; NP_811660.1; NC_004663.1.
DR RefSeq; WP_008765418.1; NC_004663.1.
DR AlphaFoldDB; Q8A455; -.
DR SMR; Q8A455; -.
DR STRING; 226186.BT_2748; -.
DR PaxDb; Q8A455; -.
DR PRIDE; Q8A455; -.
DR EnsemblBacteria; AAO77854; AAO77854; BT_2748.
DR GeneID; 60923926; -.
DR KEGG; bth:BT_2748; -.
DR PATRIC; fig|226186.12.peg.2795; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_015768_6_3_10; -.
DR InParanoid; Q8A455; -.
DR OMA; WDEGPFF; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..504
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000119509"
FT MOTIF 12..22
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT MOTIF 260..264
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ SEQUENCE 504 AA; 57734 MW; B81EB682A53E8157 CRC64;
MAERKVRVRF APSPTGALHI GGVRTALYNY LFARQHGGDL IFRIEDTDSN RFVPGAEEYI
LESFKWLGIH FDEGVSFGGE HGPYRQSERR EIYKKYVQIL LDNDKAYIAF DTPEELDAKR
AEIANFQYDA STRGMMRNSL TMSKEEVDAL IAEGKQYVVR FKIEPNEDVH VNDLIRGEVV
INSSILDDKV LYKSADELPT YHLANIVDDH LMEVSHVIRG EEWLPSAPLH VLLYRAFGWE
DTMPEFAHLP LLLKPEGNGK LSKRDGDRLG FPVFPLEWRP ESGEVSSGYR ESGYLPEAVI
NFLALLGWNP GNDQEVMSMD EMIKLFDIHR CSKSGAKFDY KKGIWFNHQY IQLKPNEEIA
ELFLPVLKEH GVEAPFEKVV TVVGMMKDRV SFIKELWDVC SFFFVAPAEY DEKTVKKRWK
EDSAKCMTEL AEVIAGIEDF SIEGQEKVVM DWIAEKGYHT GNIMNAFRLT LVGEGKGPHM
FDISWVLGKE ETLARMKRAV EVLK
