SYQ_TOLAT
ID SYQ_TOLAT Reviewed; 553 AA.
AC C4L887;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Glutamine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00126};
DE EC=6.1.1.18 {ECO:0000255|HAMAP-Rule:MF_00126};
DE AltName: Full=Glutaminyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00126};
DE Short=GlnRS {ECO:0000255|HAMAP-Rule:MF_00126};
GN Name=glnS {ECO:0000255|HAMAP-Rule:MF_00126}; OrderedLocusNames=Tola_2134;
OS Tolumonas auensis (strain DSM 9187 / TA4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Tolumonas.
OX NCBI_TaxID=595494;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9187 / TA4;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA Beller H.;
RT "Complete sequence of Tolumonas auensis DSM 9187.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-
CC glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662,
CC Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521,
CC ChEBI:CHEBI:456215; EC=6.1.1.18; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00126};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00126}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00126}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00126}.
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DR EMBL; CP001616; ACQ93733.1; -; Genomic_DNA.
DR RefSeq; WP_015879201.1; NC_012691.1.
DR AlphaFoldDB; C4L887; -.
DR SMR; C4L887; -.
DR STRING; 595494.Tola_2134; -.
DR EnsemblBacteria; ACQ93733; ACQ93733; Tola_2134.
DR KEGG; tau:Tola_2134; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_001882_2_3_6; -.
DR OMA; INNFCAQ; -.
DR OrthoDB; 142899at2; -.
DR Proteomes; UP000009073; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.1160.10; -; 1.
DR Gene3D; 2.40.240.10; -; 2.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00126; Gln_tRNA_synth; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR004514; Gln-tRNA-synth.
DR InterPro; IPR022861; Gln_tRNA_ligase_bac.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR InterPro; IPR020061; Glu_tRNA_lig_a-bdl.
DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF50715; SSF50715; 1.
DR TIGRFAMs; TIGR00440; glnS; 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..553
FT /note="Glutamine--tRNA ligase"
FT /id="PRO_1000203125"
FT MOTIF 34..44
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT MOTIF 268..272
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 35..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 41..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 67
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 212
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 261..262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 269..271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
SQ SEQUENCE 553 AA; 63541 MW; 0135C7EA14D4B9B5 CRC64;
MTQAEHRPTN FIRQIIDEDL ASGKHSSVAT RFPPEPNGYL HIGHAKSICL NFGIARDYQG
TCNLRFDDTN PVKEDVEYVE SIQRDVQWLG FEWNGAVRYS SDYFDQLHAY AIELINKGLA
YVEELTAEQI REYRGTLTQA GKNSPFRDRS VEENLALFEK MKDGGFKEGE ACLRAKIDMA
SSFMVMRDPV IYRIKFAEHH QTGNKWCIYP MYDFTHCISD ALEGITHSIC TLEFQDNRRL
YDWVLDNISI PCHPRQYEFS RLNLEYAIMS KRKLNQLVTE GVVEGWDDPR MPTVSGLRRR
GYTPEAVREF CNRIGVTKQD NTVEMSALES CIREDLNERA PRAMAVLDPL RVVLENYPED
LVEELNIPNH PNIPEAGERL VPFSREIYID RADFREEANK QYKRLVMGKE VRLRHAYIIK
AERVEKDAEG NITTLYCSCD RDTLGTNPAD GRKVKGVIHW VSAPHALDAE VRLYDRLFSV
ANPGAAEDFL STINPQSLRI VPHAKLEPSL RDAKPEFAYQ FEREGYFCAD SKLSSAEKPV
FNLTVALRDT WVG
