SYE1_HELPG
ID SYE1_HELPG Reviewed; 463 AA.
AC B5Z6J9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=HPG27_434;
OS Helicobacter pylori (strain G27).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=563041;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G27;
RX PubMed=18952803; DOI=10.1128/jb.01416-08;
RA Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S.,
RA Ottemann K.M., Stein M., Salama N.R., Guillemin K.;
RT "The complete genome sequence of Helicobacter pylori strain G27.";
RL J. Bacteriol. 191:447-448(2009).
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; CP001173; ACI27198.1; -; Genomic_DNA.
DR RefSeq; WP_000053235.1; NC_011333.1.
DR PDB; 6B1P; X-ray; 2.50 A; A=1-463.
DR PDBsum; 6B1P; -.
DR AlphaFoldDB; B5Z6J9; -.
DR SMR; B5Z6J9; -.
DR EnsemblBacteria; ACI27198; ACI27198; HPG27_434.
DR KEGG; hpg:HPG27_434; -.
DR HOGENOM; CLU_015768_6_3_7; -.
DR OMA; WDEGPFF; -.
DR OrthoDB; 1409413at2; -.
DR Proteomes; UP000001735; 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 1: Evidence at protein level;
KW 3D-structure; 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_0000367681"
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"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 18..33
FT /evidence="ECO:0007829|PDB:6B1P"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 49..65
FT /evidence="ECO:0007829|PDB:6B1P"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:6B1P"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:6B1P"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:6B1P"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:6B1P"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:6B1P"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:6B1P"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:6B1P"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:6B1P"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:6B1P"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 248..254
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 258..266
FT /evidence="ECO:0007829|PDB:6B1P"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:6B1P"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 280..286
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 301..313
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:6B1P"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 342..348
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 354..365
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 381..397
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 421..432
FT /evidence="ECO:0007829|PDB:6B1P"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 441..447
FT /evidence="ECO:0007829|PDB:6B1P"
FT HELIX 450..461
FT /evidence="ECO:0007829|PDB:6B1P"
SQ SEQUENCE 463 AA; 53318 MW; 4698E5559F338919 CRC64;
MSLIVTRFAP SPTGYLHIGG LRTAIFNYLF ARANQGKFFL RIEDTDLSRN SIEAANAIIE
AFKWVGLEYD GEILYQSKRF EIYKEYIQKL LDEDKAYYCY MSKDELDALR EEQKARKETP
RYDNRYRDFK GTPPKGIEPV VRIKVPQNEV IGFNDGVKGE VKVNTNELDD FIIARSDGTP
TYNFVVIVDD ALMGITDVIR GDDHLSNTPK QIVLYKALNF KIPNFFHVPM ILNEEGQKLS
KRHGATNVMD YQEMGYLKEA LVNFLVRLGW SYQDKEIFSM QELLECFDPK DLNSSPSCFS
WHKLNWLNAH YLKNQSAQKL LELLKPFSFS DLSHLNPAQL DRLLDALKER SQTLKELALK
IDEVLIAPVE YEEKVFKKLN QALIMPLLEK FKLELKEANF NDESALENAM HKIIEEEKIK
AGSFMQPLRL ALLGKGGGIG LKEALFILGK TESVKRIENF LKN
