ID   GLUQ_BIFLO              Reviewed;         379 AA.
AC   Q8G4X3;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Glutamyl-Q tRNA(Asp) synthetase;
DE            Short=Glu-Q-RSs;
DE            EC=6.1.1.-;
GN   Name=gluQ; OrderedLocusNames=BL1251;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
CC   -!- FUNCTION: Catalyzes the tRNA-independent activation of glutamate in
CC       presence of ATP and the subsequent transfer of glutamate onto a
CC       tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-
CC       cyclopenten-1-yl) moiety of the queuosine in the wobble position of the
CC       QUC anticodon (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       GluQ subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014295; AAN25052.1; -; Genomic_DNA.
DR   RefSeq; NP_696416.1; NC_004307.2.
DR   AlphaFoldDB; Q8G4X3; -.
DR   SMR; Q8G4X3; -.
DR   STRING; 206672.BL1251; -.
DR   EnsemblBacteria; AAN25052; AAN25052; BL1251.
DR   KEGG; blo:BL1251; -.
DR   PATRIC; fig|206672.9.peg.1536; -.
DR   HOGENOM; CLU_015768_0_0_11; -.
DR   OMA; WLLRMED; -.
DR   PhylomeDB; Q8G4X3; -.
DR   Proteomes; UP000000439; Chromosome.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043039; P:tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00749; tRNA-synt_1c; 2.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Zinc.
FT   CHAIN           1..379
FT                   /note="Glutamyl-Q tRNA(Asp) synthetase"
FT                   /id="PRO_0000208287"
FT   REGION          161..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           17..27
FT                   /note="'HIGH' region"
FT   MOTIF           300..304
FT                   /note="'KMSKS' region"
FT   BINDING         14..18
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         50
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   379 AA;  42168 MW;  DEAC7D620B757C8B CRC64;
     MVLNFIRGGP VTGRFAPTPS GRMHIGNVYA MLGAWLSARS RGDRMLMRIE DVDKPRVVAG
     ADQLMMDDLH WLGLDWDGEP MFQSQRTERY EYALECLRSQ GVLYPCFCSR ADIRAASAPN
     EGDGFMVYPG TCRRLLHDHP DEVRARLVRG DQHSIRIAMP ESAAGEKQRT VPDDSAALSG
     AVPPEQQGDA GIVDGVACFN DRVYSPQHYD LAREVGDSVI RRADGLFGYQ LVVVVDDLDM
     GVDDIVRGRD LLRSTALQMW IRQCLLAGGF EPECGNTEKP LAEHPEYAHL PLIDNAAGRR
     LAKRERSLDM GALRARNVTP EQIIGYCAWL LRLQPTPIPC KPADLLADFS WEPLRANHLD
     RALKPDDPTT PQWLAEALG