SYQ_CLOK5
ID SYQ_CLOK5 Reviewed; 556 AA.
AC A5N6Y3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=CKL_1022;
OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=431943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680;
RX PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA Hagemeier C., Thauer R.K., Gottschalk G.;
RT "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT metabolic features.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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; CP000673; EDK33064.1; -; Genomic_DNA.
DR RefSeq; WP_012101396.1; NC_009706.1.
DR AlphaFoldDB; A5N6Y3; -.
DR SMR; A5N6Y3; -.
DR STRING; 431943.CKL_1022; -.
DR EnsemblBacteria; EDK33064; EDK33064; CKL_1022.
DR KEGG; ckl:CKL_1022; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_001882_2_3_9; -.
DR OMA; INNFCAQ; -.
DR OrthoDB; 142899at2; -.
DR Proteomes; UP000002411; 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; 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; 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..556
FT /note="Glutamine--tRNA ligase"
FT /id="PRO_1000095483"
FT MOTIF 33..43
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT MOTIF 266..270
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 34..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 40..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 66
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 210
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 259..260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 267..269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
SQ SEQUENCE 556 AA; 64440 MW; F54B497C7FBED2F5 CRC64;
MGDNNNSSNF IKNIIIEDLK SGEYEKVVTR FPPEPNGYLH IGHAKSIVLN FSLADEFEGK
VNLRFDDTNP SKEDVEYVES IKEDVKWLGY NWDNLCFASS YFERMYEYAV FLIKKGKAYV
CDLTADEIRE YRGTLTKPGK ESPYRNRDVE ENFKLFEGMK NGEFKDGEKV LRAKIDMASP
NINMRDPVLY RIAHASHHNT GDRWCIYPMY DFAHPLEDAI EGVTHSICTL EFEDHRPLYD
WIIQECEIEN RPKQIEFARL NMTNTVMSKR KLKQLVDENF VDGWDDPRMP TIAGLRRRGF
TPESIRNFCR AIGVSKASSI VDSQMLDYFL RDDLEKEAPR TMAILNPLKV VITNYPEGKT
ETFKIENNPD DASAGVREVP FSREIYIEQE DFMENPPKKY YRLFPGNEVR LKSAYFIKCT
EAIKDKDGNV IELRCTYDPA SKGGNSPDGR KVRGTLHWIN VDTAIPAEIR LYEPLILEQQ
EKEGEEDLFL DHVNPNSLKV VKGFVEPDMK HVKSDEKFQF FRHGYFVLDG KCSKNGELVF
NRIVSLKSSF KIPENK
