SYE_THEVB
ID SYE_THEVB Reviewed; 485 AA.
AC Q8DLI5;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=tll0506;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH GLUTAMATE, FUNCTION,
RP ABSENCE OF COFACTOR REQUIREMENT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16876193; DOI=10.1016/j.jmb.2006.06.054;
RA Schulze J.O., Masoumi A., Nickel D., Jahn M., Jahn D., Schubert W.-D.,
RA Heinz D.W.;
RT "Crystal structure of a non-discriminating glutamyl-tRNA synthetase.";
RL J. Mol. Biol. 361:888-897(2006).
CC -!- FUNCTION: Non-discriminating glutamyl-tRNA synthetase. Catalyzes the
CC attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate
CC is first activated by ATP to form Glu-AMP and then transferred to the
CC acceptor end of tRNA(Glu). Acylates both tRNA(Glu) and tRNA(Gln) with
CC glutamate, but has 13-fold higher efficiency with tRNA(Glu).
CC {ECO:0000269|PubMed:16876193}.
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 -!- COFACTOR:
CC Note=Does not require zinc.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.79 uM for tRNA-Glu {ECO:0000269|PubMed:16876193};
CC KM=3.7 uM for tRNA-Gln {ECO:0000269|PubMed:16876193};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: This organism lacks a tRNA synthetase for tRNA(Gln).
CC Instead, tRNA(Gln) is first charged with Glu, and then the bound
CC glutamate is converted to glutamine by GatCAB.
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; BA000039; BAC08058.1; -; Genomic_DNA.
DR RefSeq; NP_681296.1; NC_004113.1.
DR RefSeq; WP_011056357.1; NC_004113.1.
DR PDB; 2CFO; X-ray; 2.45 A; A/B=2-485.
DR PDBsum; 2CFO; -.
DR AlphaFoldDB; Q8DLI5; -.
DR SMR; Q8DLI5; -.
DR STRING; 197221.22294227; -.
DR EnsemblBacteria; BAC08058; BAC08058; BAC08058.
DR KEGG; tel:tll0506; -.
DR PATRIC; fig|197221.4.peg.533; -.
DR eggNOG; COG0008; Bacteria.
DR OMA; WDEGPFF; -.
DR OrthoDB; 1409413at2; -.
DR SABIO-RK; Q8DLI5; -.
DR EvolutionaryTrace; Q8DLI5; -.
DR Proteomes; UP000000440; 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:UniProtKB-UniRule.
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; 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; 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; Reference proteome.
FT CHAIN 1..485
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000119674"
FT MOTIF 9..19
FT /note="'HIGH' region"
FT MOTIF 248..252
FT /note="'KMSKS' region"
FT BINDING 6
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:16876193"
FT BINDING 192
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:16876193"
FT BINDING 210..214
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 17..32
FT /evidence="ECO:0007829|PDB:2CFO"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2CFO"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:2CFO"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:2CFO"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:2CFO"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:2CFO"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:2CFO"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:2CFO"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:2CFO"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:2CFO"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 192..202
FT /evidence="ECO:0007829|PDB:2CFO"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 212..216
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 217..227
FT /evidence="ECO:0007829|PDB:2CFO"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:2CFO"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:2CFO"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 292..298
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 313..324
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 329..342
FT /evidence="ECO:0007829|PDB:2CFO"
FT TURN 349..352
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 353..363
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 373..381
FT /evidence="ECO:0007829|PDB:2CFO"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 389..395
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 400..410
FT /evidence="ECO:0007829|PDB:2CFO"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 419..433
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 437..449
FT /evidence="ECO:0007829|PDB:2CFO"
FT STRAND 450..453
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 457..466
FT /evidence="ECO:0007829|PDB:2CFO"
FT HELIX 470..484
FT /evidence="ECO:0007829|PDB:2CFO"
SQ SEQUENCE 485 AA; 54362 MW; C3547C6415FDDCBA CRC64;
MTVRVRLAPS PTGNLHIGTA RTAVFNWLYA RHRGGKFILR IEDTDRERSR PEYTENILEG
LQWLGLTWDE GPYFQSDRLD LYRQAIQTLL DKGLAYYCYC TPEELEALRA EQKAKGQAPR
YDNRHRHLTP EEQAAFEAAG RTPVIRFKIE DDRQIEWQDL VRGRVSWQGA DLGGDMVIAR
AAPRGEIGYP LYNLVVVVDD IAMGITDVIR GEDHIGNTPK QILLYEALGA TPPNFAHTPL
ILNSTGQKLS KRDGVTSISD FRAMGYLAPA LANYMTLLGW SPPEGVGELF TLDLAAKHFS
FERINKAGAR FDWDKLNWLN RQYIQQLEPE EFLAELIPLW QGAGYAFDEE RDRPWLFDLA
QLLQPGLNTL REAIDQGAVF FIPSVTFDSE AMAQLGQPQS ATILAYLLEH LPAEPALTVA
MGQQLIQQAA KAAGVKKGAT MRTLRAALTG AVHGPDLMAA WQILHQRGWD EPRLAAALKQ
AQTTS
