ID   SYE_TRIEI               Reviewed;         881 AA.
AC   Q119Z5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   24-JAN-2024, entry version 105.
DE   RecName: Full=Glutamate--tRNA ligase;
DE            EC=6.1.1.17;
DE   AltName: Full=Glutamyl-tRNA synthetase;
DE            Short=GluRS;
GN   Name=gltX; OrderedLocusNames=Tery_0188;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RX   PubMed=25831533; DOI=10.1073/pnas.1422332112;
RA   Walworth N., Pfreundt U., Nelson W.C., Mincer T., Heidelberg J.F., Fu F.,
RA   Waterbury J.B., Glavina del Rio T., Goodwin L., Kyrpides N.C., Land M.L.,
RA   Woyke T., Hutchins D.A., Hess W.R., Webb E.A.;
RT   "Trichodesmium genome maintains abundant, widespread noncoding DNA in situ,
RT   despite oligotrophic lifestyle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:4251-4256(2015).
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:0000250}.
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;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       Glutamate--tRNA ligase type 1 subfamily. {ECO:0000305}.
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DR   EMBL; CP000393; ABG49679.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q119Z5; -.
DR   SMR; Q119Z5; -.
DR   STRING; 203124.Tery_0188; -.
DR   KEGG; ter:Tery_0188; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_015768_4_0_3; -.
DR   OrthoDB; 9807503at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; 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; 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; IPR025564; CAAD_dom.
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   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; PF14159; CAAD; 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; ATP-binding; Cell membrane; Cytoplasm; Ligase;
KW   Membrane; Nucleotide-binding; Protein biosynthesis; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..881
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_0000367797"
FT   TRANSMEM        809..829
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        832..852
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..480
FT                   /note="Glutamyl-tRNA synthetase"
FT   REGION          481..881
FT                   /note="Unknown"
FT   REGION          488..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           9..19
FT                   /note="'HIGH' region"
FT   MOTIF           248..252
FT                   /note="'KMSKS' region"
FT   COMPBIAS        505..747
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         251
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   881 AA;  98269 MW;  1C675432E0CA07E9 CRC64;
     MSVRVRLAPS PTGNLHIGTA RTAVFNWLFA RNQKGKFILR IEDTDQERSR PEYTDNILEG
     LSWLGLEWDE GPFYQCQRYE LYQKATQSLL DKGLAYRCYC TAAELEEMRE AQKARKEAPR
     YDNRHRNLTD LEKKAFEAEG RQAVIRFRID DDQIITWNDM VRGKVTWKGS DLGGDMVISR
     AAGGDEVGQP LYNMAVVVDD MDMEITHVIR GEDHIANTAK QILLYEALGG KIPEFGHTPL
     ILNKEGRKLS KRDGVTSISD FQELGFTPEA LANYMCLLGW TPPDATEEIF TLAQAGQNFS
     FERVNKAGAK FDWDKLDWIS SQYLHNLPVK QLTDKLIPIW QKAGYELDPE GDRSWLEQLV
     TLIRPSLTRL TDAVEMSELF FFPTVELNED AKTQMQNEDS VKSINSILEI INADAPLLVA
     DVKQTIKKVT QKVHVKKGVV MRSLRASLTG AMQGPDLIES WLLLHQKGFD ILRFKKSIGQ
     EIEDTKIEDT KKAETTPHKS KGEGNVLLKT TTPKSPALSK EQTQTTKPPK KGQTATPVAT
     TPTATDVTEN TSVGTQETQS QITTPVATTP TATDVTENTS VGTQETQSQI TTPVATTPTA
     TDVTENTSVE TQETQSQITT PVATTPTATD VTENTSVETQ ETQSQITTPV ATTPTATDVT
     ENTSVGTQET QSQITTPVAT TPTATDVTEN TSVETQETQS QITTPVATTS TATDVTENTS
     VETQETQSQI TTPVATTPTA TDAETREQKV ATQVETSILD DQKPVDTVTN QTVEVEQPNK
     IKEQFINIFF NFPDYINQLY QQYQGQLKLF GWLALVILTF TFMAVVIEAL DGIPILSIIF
     ELIGVIYLVW FVYRYLLKRS NRQELLDKIE NIKREIFGKP S
//