ID   D1CDJ3_THET1            Unreviewed;       492 AA.
AC   D1CDJ3;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   04-NOV-2026, entry version 97.
DE   RecName: Full=Glutamate--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00022};
DE            EC=6.1.1.17 {ECO:0000256|HAMAP-Rule:MF_00022};
DE   AltName: Full=Glutamyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00022};
DE            Short=GluRS {ECO:0000256|HAMAP-Rule:MF_00022};
GN   Name=gltX {ECO:0000256|HAMAP-Rule:MF_00022};
GN   OrderedLocusNames=Tter_0077 {ECO:0000313|EMBL:ACZ40999.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / CCMEE 7001 / YNP1).
OC   Bacteria; Bacillati; Chloroflexota; Chloroflexia;
OC   Candidatus Thermobaculales; Candidatus Thermobaculaceae; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ40999.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y., Jeffries C., Lu M., Brettin T., Detter J., Goker M.,
RA   Tindall B., Beck B., McDermott T., Woyke T., Bristow J., Eisen J.,
RA   Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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:0000256|HAMAP-
CC       Rule:MF_00022}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Glu) + L-glutamate + ATP = L-glutamyl-tRNA(Glu) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663, Rhea:RHEA-
CC         COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78520, ChEBI:CHEBI:456215;
CC         EC=6.1.1.17; Evidence={ECO:0000256|HAMAP-Rule:MF_00022};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00022}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00022}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       Glutamate--tRNA ligase type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007894, ECO:0000256|HAMAP-Rule:MF_00022}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-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; CP001825; ACZ40999.1; -; Genomic_DNA.
DR   RefSeq; WP_012874034.1; NC_013525.1.
DR   AlphaFoldDB; D1CDJ3; -.
DR   STRING; 525904.Tter_0077; -.
DR   KEGG; ttr:Tter_0077; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_015768_6_3_0; -.
DR   OMA; AADDHYM; -.
DR   OrthoDB; 9807503at2; -.
DR   Proteomes; UP000000323; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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   FunFam; 3.40.50.620:FF:000045; Glutamate--tRNA ligase, mitochondrial; 1.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 1.10.8.70; Glutamate-tRNA synthetase, class I, anticodon-binding domain 1; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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; IPR049940; GluQ/Sye.
DR   InterPro; IPR033910; GluRS_core.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00464; gltX_bact; 1.
DR   PANTHER; PTHR43311; GLUTAMATE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43311:SF2; GLUTAMATE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF19269; Anticodon_2; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00022};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00022};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00022};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00022};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00022};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00022}; Reference proteome {ECO:0000313|Proteomes:UP000000323}.
FT   DOMAIN          4..321
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          336..482
FT                   /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19269"
FT   MOTIF           11..21
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
FT   MOTIF           252..256
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
FT   BINDING         255
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
SQ   SEQUENCE   492 AA;  55666 MW;  6F0374557C5527BA CRC64;
     MNSEVRVRFP PSPTGYLHVG NLRTAVFNWL LARHHGGKFI LRIEDTDRAR VVPGAVEVIY
     ETLRWIGIDW DEGPDIGGPH APYVQSERKE IYREYAELLI SQGKAYRCFC SQERLEALRE
     EQRKNNLPTR YDRKCRYLGP EEAKRLVDSG QPYVVRFATP LEGTTTMVDL LRGPVTYQND
     QIDDFVILKS DGYPPYHFAV VVDDHLMGIT HVLRGDEYIS SGARDILLHE ALGWNPPLYA
     HTAIILGPDR SRLSKRHGAL PALEYRDIGI IPEAMFNYLA LLGASYSADR EIFSREELIE
     LFDIDKMSPS PAIFDANKLE WMNAYYINHV LSVDDLASRV KPILENAGLV KTEDLDEGYL
     IEVIGLVKDR IKLLPDVVEL TDFFFRDPDP SAEEIAGKKL TLQEAQELLQ KVKDRVSPID
     NWSEEILETE LRSMASELGV KTGTLFMLIR VAITGKTASP GLFETMAVLG KDRTISRIGR
     AIDKLDLVVH GG
//