ID   GLUQ_RHOCB              Reviewed;         278 AA.
AC   O68142; D5AUR6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 2.
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=RCAP_rcc01961;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=9256491; DOI=10.1073/pnas.94.17.9384;
RA   Vlcek C., Paces V., Maltsev N., Paces J., Haselkorn R., Fonstein M.;
RT   "Sequence of a 189-kb segment of the chromosome of Rhodobacter capsulatus
RT   SB1003.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:9384-9388(1997).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAC16232.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001312; ADE85705.1; -; Genomic_DNA.
DR   EMBL; AF010496; AAC16232.1; ALT_INIT; Genomic_DNA.
DR   PIR; T03579; T03579.
DR   RefSeq; WP_013067684.1; NC_014034.1.
DR   AlphaFoldDB; O68142; -.
DR   SMR; O68142; -.
DR   STRING; 272942.RCAP_rcc01961; -.
DR   EnsemblBacteria; ADE85705; ADE85705; RCAP_rcc01961.
DR   GeneID; 31490829; -.
DR   KEGG; rcp:RCAP_rcc01961; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_015768_0_3_5; -.
DR   OMA; WLLRMED; -.
DR   OrthoDB; 1409413at2; -.
DR   Proteomes; UP000002361; Chromosome.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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.
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..278
FT                   /note="Glutamyl-Q tRNA(Asp) synthetase"
FT                   /id="PRO_0000119635"
FT   MOTIF           7..17
FT                   /note="'HIGH' region"
FT   MOTIF           249..253
FT                   /note="'KMSKS' region"
FT   BINDING         4..8
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         193
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         211
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         252
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   278 AA;  30842 MW;  042107F50248DB96 CRC64;
     MITRFAPSPT GPLHLGHAFA AILAHDMARA AGGRFLLRIE DIDRARAKPQ WEAQLLDDLR
     WLGITWDGPV LRQSDRLPLY RDALERLWQR GLVYSCTCSR RDIEQAASAP QEGAPLGPDG
     IVYPGSCRDK GRPRPGQALP ETALRLRMDL AATETGFEET GPAHRGWHEI RPETMIRAVG
     DVVLARREMG TSYHLSVVLD DAAQGVTHVT RGEDLFEATC IHVTLQRLLG LPVPVYHHHG
     LIRDDAGKRL AKRDNARALS KYRAEGASPA DIRRLIGL