SYE1_HELP2
ID SYE1_HELP2 Reviewed; 463 AA.
AC B6JL62;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=HPP12_0486;
OS Helicobacter pylori (strain P12).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=570508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P12;
RA Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.;
RT "The complete genome sequence of Helicobacter pylori strain P12.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001217; ACJ07640.1; -; Genomic_DNA.
DR RefSeq; WP_000053249.1; NC_011498.1.
DR AlphaFoldDB; B6JL62; -.
DR SMR; B6JL62; -.
DR EnsemblBacteria; ACJ07640; ACJ07640; HPP12_0486.
DR KEGG; hpp:HPP12_0486; -.
DR HOGENOM; CLU_015768_6_3_7; -.
DR OMA; HYINTLP; -.
DR OrthoDB; 1409413at2; -.
DR Proteomes; UP000008198; 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; 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.
FT CHAIN 1..463
FT /note="Glutamate--tRNA ligase 1"
FT /id="PRO_0000367685"
FT MOTIF 10..20
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT MOTIF 238..242
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ SEQUENCE 463 AA; 53377 MW; F15DBFF3C85C6F5D CRC64;
MSLIVTRFAP SPTGYLHIGG LRTAIFNYLF ARANQGKFFL RIEDTDLSRN SIEAANAIIE
AFKWVGLEYD GEILYQSKRF EIYKEYIQKL LDEDKAYYCY MSKYELDALR EEQKARKETP
RYDNRYRDFK GTPPKGIEPV VRIKVPQNEV IGFNDGVKGE VRVNTNELDD FIIARSDGVP
TYNFVVTIDD ALMGITDVIR GDDHLSNTPK QIVLYKALNF KIPNFFHVPM ILNEEGQKLS
KRHGATNVMD YQERGYLKEA LVNFLARLGW SYQDKEIFSM QELLECFDPK DLNSSPSCFS
WHKLNWLNAH YLKNQSTQEL LKLLKPFSFS DLSHLNPAQL DRLLDALKER SQTLKELALK
IDEVLTAPIE YEEKVLKKLN QALVMPLLEK FKLELNTTNF NDESALENAM HQIIEEEKIK
AGSFMQPLRL ALLGKGGGIG LKEALFILGK TESVKRIEKF LKN
