(data stored in ACNUC7421 zone)

SWISSPROT: SYQ_ECO27

ID   SYQ_ECO27               Reviewed;         554 AA.
AC   B7UKW1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 65.
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=E2348C_0571;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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
CC       family. {ECO:0000255|HAMAP-Rule:MF_00126}.
DR   EMBL; FM180568; CAS08119.1; -; Genomic_DNA.
DR   RefSeq; WP_001287134.1; NC_011601.1.
DR   SMR; B7UKW1; -.
DR   PRIDE; B7UKW1; -.
DR   EnsemblBacteria; CAS08119; CAS08119; E2348C_0571.
DR   KEGG; ecg:E2348C_0571; -.
DR   KO; K01886; -.
DR   OMA; VTHSICT; -.
DR   BioCyc; ECOL574521:E2348C_RS03025-MONOMER; -.
DR   Proteomes; UP000008205; 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;
DR   PRODOM; B7UKW1.
DR   SWISS-2DPAGE; B7UKW1.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    554       Glutamine--tRNA ligase.
FT                                /FTId=PRO_1000199095.
FT   NP_BIND      35     37       ATP. {ECO:0000255|HAMAP-Rule:MF_00126}.
FT   NP_BIND      41     47       ATP. {ECO:0000255|HAMAP-Rule:MF_00126}.
FT   NP_BIND     261    262       ATP. {ECO:0000255|HAMAP-Rule:MF_00126}.
FT   NP_BIND     269    271       ATP. {ECO:0000255|HAMAP-Rule:MF_00126}.
FT   REGION      317    324       Interaction with tRNA.
FT                                {ECO:0000255|HAMAP-Rule:MF_00126}.
FT   MOTIF        34     44       "HIGH" region. {ECO:0000255|HAMAP-
FT                                Rule:MF_00126}.
FT   MOTIF       268    272       "KMSKS" region. {ECO:0000255|HAMAP-
FT                                Rule:MF_00126}.
FT   BINDING      67     67       L-glutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00126}.
FT   BINDING     212    212       L-glutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00126}.
FT   BINDING     231    231       ATP. {ECO:0000255|HAMAP-Rule:MF_00126}.
SQ   SEQUENCE   554 AA;  63494 MW;  FE93254893E811F9 CRC64;
     MSEAEARPTN FIRQIIDEDL ASGKHTTVHT RFPPEPNGYL HIGHAKSICL NFGIAQDYKG
     QCNLRFDDTN PVKEDIEYVD SIKNDVEWLG FHWSGNVRYS SDYFDQLHAY AIELINKGLA
     YVDELTPEQI REYRGTLTQP GKNSPYRDRS VEENLALFEK MRTGGFEEGK ACLRAKIDMA
     SPFIVMRDPV LYRIKFAEHH QTGNKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL
     YDWVLDNITI PVHPRQYEFS RLNLEYTVMS KRKLNLLVTD KHVEGWDDPR MPTISGLRRR
     GYTAASIREF CKRIGVTKQD NTIEMASLES CIREDLNENA PRAMAVIDPV KLVIENYQGE
     GEMVTMPNHP NKPEMGSRQV PFSGEIWIDR ADFREEANKQ YKRLVLGKEV RLRNAYVIKA
     ERVEKDAEGN ITTIFCTYDA DTLSKDPADG RKVKGVIHWV SAAHALPVEI RLYDRLFSVP
     NPGAADDFLS VINPESLVIK QGFAEPSLKD AVAGKAFQFE REGYFCLDSR HSTAEKPVFN
     RTVGLRDTWA KVGE
//

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