ID   SYQ_HAEDU               Reviewed;         556 AA.
AC   Q7VLM3;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 117.
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};
GN   OrderedLocusNames=HD_1404;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) 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; AE017143; AAP96212.1; -; Genomic_DNA.
DR   RefSeq; WP_010945261.1; NC_002940.2.
DR   AlphaFoldDB; Q7VLM3; -.
DR   SMR; Q7VLM3; -.
DR   STRING; 233412.HD_1404; -.
DR   KEGG; hdu:HD_1404; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_001882_2_3_6; -.
DR   OrthoDB; 9801560at2; -.
DR   Proteomes; UP000001022; 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   CDD; cd00807; GlnRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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_bL25/Gln-tRNA_synth_N.
DR   InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR049437; tRNA-synt_1c_C2.
DR   NCBIfam; TIGR00440; glnS; 1.
DR   PANTHER; PTHR43097:SF4; GLUTAMINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 1.
DR   Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50715; Ribosomal protein L25-like; 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_0000195836"
FT   MOTIF           39..49
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   MOTIF           274..278
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         40..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         46..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         72
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         217
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         267..268
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
SQ   SEQUENCE   556 AA;  63897 MW;  8317AA836D7092CC CRC64;
     MSEETLTTEV ETRTNFITHI IDEDLASGKH NNVYTRFPPE PNGYLHIGHA KSICLNFGIA
     QEYHGKCNLR FDDTNPVKED IEYVASIKQD VEWLGFKWQG EPRYASDYFD QLHGYAIELI
     EKGLAYVDEL SPEEMREYRG TLTEAGKNSP YRDRSIAENL ALFEKMKNGE FKEGTACLRA
     KIDMASPFIV MRDPVLYRVK FAHHHQTGDK WCIYPMYDFT HCISDAIERI THSLCTLEFQ
     DNRRLYDWVL ENISIERPLP HQYEFSRLNL EGTLTSKRKL LQLVTDGIVD GWNDPRMPTI
     SGLRRRGYTP ASLREFCRRI GVTKQDNVVE YAALEACIRE DLNENAPRAM AVINPVRVVI
     ENVAEPEILK APNHPNRPEL GERDLPFTRE IYIDEADFRE EANKQYKRLV LGKEVRLRNA
     YVIKAERVEK DASGKITTIF CSYDPETLGK NPADGRKVKG VIHWVSATQN KVAEFRIYNR
     LFNVANPGDE EDINAVINPS SLIVKHGFVE VNLANAQKEQ GYQFEREGYY CLDSKEGSAD
     NLIFNLTVSL KEGFTA
//