SYE1_THEP3
ID SYE1_THEP3 Reviewed; 485 AA.
AC B0KCH7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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};
GN OrderedLocusNames=Teth39_0351;
OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS thermohydrosulfuricum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=340099;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33223 / DSM 2355 / 39E;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J.,
RA Richardson P.;
RT "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
RL Submitted (JAN-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}.
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DR EMBL; CP000924; ABY94020.1; -; Genomic_DNA.
DR RefSeq; WP_012268987.1; NC_010321.1.
DR AlphaFoldDB; B0KCH7; -.
DR SMR; B0KCH7; -.
DR STRING; 340099.Teth39_0351; -.
DR EnsemblBacteria; ABY94020; ABY94020; Teth39_0351.
DR KEGG; tpd:Teth39_0351; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_015768_6_3_9; -.
DR OMA; WDEGPFF; -.
DR Proteomes; UP000002156; 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; Reference proteome.
FT CHAIN 1..485
FT /note="Glutamate--tRNA ligase 1"
FT /id="PRO_0000367781"
FT MOTIF 10..20
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT MOTIF 252..256
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ SEQUENCE 485 AA; 56418 MW; 73AD9CC644ECBC48 CRC64;
MNNLRVRFAP SPTGAIHIGN IRTALFNYLF SRSEGATFVL RIEDTDLERS SKEFEELIFK
ELEWLGIEWD EGPDKPGPYG PYRQSERLEI YHKFAQKLIE EKKAYRCYCT PEELEEDRRK
AVERGDIPCY SGRCRYLTKE QEEAFIREGR KPVIRFIIPD DEVIEFEDMI KGKITIKSDT
LGGDMVIVKS DGMPTYNFAV VIDDALMKIT HVIRGEDHIY NTPKQILIYK ALGFEIPKFA
HAPLILGPDR TKLSKRHGNT YIGQYRELGY LPEAMFNFLS LLSWSPEDNV EIMSKEEIIK
KFNFRRIHSA NPVFDIEKLN WMNQQYIQKS SIERIVDLAI PHLRRAGYID GIDDMVYNWL
KDVISLYKDG LQYVAQITEK AKMFFVEEVE YSDETVKILN SPNSKIVLEV VKKVIEEADE
ITEEYVKDLL KKLQKETKVK GKEFFMPIRV AITGEDHGPE LVKIIPLLGK DKVINRLKKA
INLIK
