SYE1_THEMA
ID SYE1_THEMA Reviewed; 469 AA.
AC Q9X172;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Glutamate--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00022};
DE EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022};
DE AltName: Full=Glutamyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00022};
DE Short=GluRS 1 {ECO:0000255|HAMAP-Rule:MF_00022};
GN Name=gltX1 {ECO:0000255|HAMAP-Rule:MF_00022}; OrderedLocusNames=TM_1351;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS).
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of glutamyl-tRNA synthetase 1 (EC 6.1.1.17) (glutamate-
RT tRNA ligase 1) (glurS 1) (TM1351) from Thermotoga maritima at 2.5 A
RT resolution.";
RL Submitted (DEC-2006) to the PDB data bank.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000512; AAD36422.1; -; Genomic_DNA.
DR PIR; G72264; G72264.
DR RefSeq; NP_229152.1; NC_000853.1.
DR RefSeq; WP_004081547.1; NZ_CP011107.1.
DR PDB; 2O5R; X-ray; 2.34 A; A=1-469.
DR PDBsum; 2O5R; -.
DR AlphaFoldDB; Q9X172; -.
DR SMR; Q9X172; -.
DR STRING; 243274.THEMA_07585; -.
DR EnsemblBacteria; AAD36422; AAD36422; TM_1351.
DR KEGG; tma:TM1351; -.
DR eggNOG; COG0008; Bacteria.
DR InParanoid; Q9X172; -.
DR OMA; HYINTLP; -.
DR OrthoDB; 1409413at2; -.
DR EvolutionaryTrace; Q9X172; -.
DR Proteomes; UP000008183; 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; 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; 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; 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.
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..469
FT /note="Glutamate--tRNA ligase 1"
FT /id="PRO_0000119680"
FT MOTIF 8..18
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT MOTIF 250..254
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 16..32
FT /evidence="ECO:0007829|PDB:2O5R"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:2O5R"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2O5R"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:2O5R"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:2O5R"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:2O5R"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:2O5R"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:2O5R"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:2O5R"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:2O5R"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:2O5R"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:2O5R"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 217..229
FT /evidence="ECO:0007829|PDB:2O5R"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:2O5R"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 260..266
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 270..278
FT /evidence="ECO:0007829|PDB:2O5R"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 293..299
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 314..327
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 330..343
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 351..361
FT /evidence="ECO:0007829|PDB:2O5R"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 371..374
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 392..401
FT /evidence="ECO:0007829|PDB:2O5R"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 409..423
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 427..438
FT /evidence="ECO:0007829|PDB:2O5R"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 447..453
FT /evidence="ECO:0007829|PDB:2O5R"
FT HELIX 456..466
FT /evidence="ECO:0007829|PDB:2O5R"
SQ SEQUENCE 469 AA; 54607 MW; F27D3AB4FE070BD8 CRC64;
MVRVRFAPSP TGFLHVGGAR TALFNFLFAR KEKGKFILRI EDTDLERSER EYEEKLMESL
RWLGLLWDEG PDVGGDHGPY RQSERVEIYR EHAERLVKEG KAYYVYAYPE EIEEMREKLL
SEGKAPHYSQ EMFEKFDTPE RRREYEEKGL RPAVFFKMPR KDYVLNDVVK GEVVFKTGAI
GDFVIMRSNG LPTYNFACVV DDMLMEITHV IRGDDHLSNT LRQLALYEAF EKAPPVFAHV
STILGPDGKK LSKRHGATSV EAFRDMGYLP EALVNYLALL GWSHPEGKEL LTLEELISSF
SLDRLSPNPA IFDPQKLKWM NGYYLRNMPI EKLAELAKPF FEKAGIKIID EEYFKKVLEI
TKERVEVLSE FPEESRFFFE DPAPVEIPEE MKEVFSQLKE ELQNVRWTME EITPVFKKVL
KQHGVKPKEF YMTLRRVLTG REEGPELVNI IPLLGKEIFL RRIERSLGG
