ID   GLUQ_PSYA2              Reviewed;         335 AA.
AC   Q4FQ23;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Glutamyl-Q tRNA(Asp) synthetase;
DE            Short=Glu-Q-RSs;
DE            EC=6.1.1.-;
GN   Name=gluQ; OrderedLocusNames=Psyc_2038;
OS   Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=259536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17307 / VKM B-2377 / 273-4;
RX   PubMed=20154119; DOI=10.1128/aem.02101-09;
RA   Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA   Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA   Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA   Murray A., Thomashow M., Tiedje J.M.;
RT   "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT   Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT   temperature growth.";
RL   Appl. Environ. Microbiol. 76:2304-2312(2010).
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}.
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DR   EMBL; CP000082; AAZ19885.1; -; Genomic_DNA.
DR   RefSeq; WP_011281292.1; NC_007204.1.
DR   AlphaFoldDB; Q4FQ23; -.
DR   SMR; Q4FQ23; -.
DR   STRING; 259536.Psyc_2038; -.
DR   EnsemblBacteria; AAZ19885; AAZ19885; Psyc_2038.
DR   KEGG; par:Psyc_2038; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_015768_0_1_6; -.
DR   OMA; DADTERC; -.
DR   OrthoDB; 1409413at2; -.
DR   Proteomes; UP000000546; 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; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Zinc.
FT   CHAIN           1..335
FT                   /note="Glutamyl-Q tRNA(Asp) synthetase"
FT                   /id="PRO_0000208319"
FT   MOTIF           16..26
FT                   /note="'HIGH' region"
FT   MOTIF           268..272
FT                   /note="'KMSKS' region"
FT   BINDING         13..17
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         49
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         211
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   335 AA;  38100 MW;  FA1E5EB102B0C39E CRC64;
     MPITRTLPQP IGRFAPSPTG ELHLGSLTTA LASFCHIKSI DGKWLLRIED TDTERCDRQF
     TEQILIDLEA LGLNWDDDVI FQSERIDIYN DYISSVLRPL TYSCQCSRKR LERYWTQQEQ
     QTALTDANIS TDLSVSVNND KRVDSHLLPN RQRYPRFCIK ANLSPTQNKL RIQLPDYCIG
     FNDGIQGIQW DNPQQTLGDM VARRQDGMIN YILAASLDDG LQQVTHIMRG LDILPMTTAQ
     ISIMQAARLP TISHWYHLPL ICNPDGQKLS KQNLAQPIDT RHPSKLLAYA LKLLGQLPVD
     HDTPERMLNQ AISQWDNAPL QGRQSLNMAT IVGEK