SYE_TRIEI
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 03-AUG-2022, entry version 99.
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; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Microcoleaceae; Trichodesmium.
OX NCBI_TaxID=203124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMS101;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Richardson P.;
RT "Complete sequence of Trichodesmium erythraeum IMS101.";
RL Submitted (JUN-2006) 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: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 PRIDE; Q119Z5; -.
DR EnsemblBacteria; ABG49679; ABG49679; Tery_0188.
DR KEGG; ter:Tery_0188; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_015768_4_0_3; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 1.10.1160.10; -; 1.
DR Gene3D; 1.10.8.70; -; 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; 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 Pfam; PF19269; Anticodon_2; 1.
DR Pfam; PF14159; CAAD; 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; 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
