ID   GLUQ_CUTAK              Reviewed;         347 AA.
AC   Q6A7Y1;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Glutamyl-Q tRNA(Asp) synthetase {ECO:0000255|HAMAP-Rule:MF_01428};
DE            Short=Glu-Q-RSs {ECO:0000255|HAMAP-Rule:MF_01428};
DE            EC=6.1.1.- {ECO:0000255|HAMAP-Rule:MF_01428};
GN   Name=gluQ {ECO:0000255|HAMAP-Rule:MF_01428}; OrderedLocusNames=PPA1383;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
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. {ECO:0000255|HAMAP-Rule:MF_01428}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01428};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01428};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       GluQ subfamily. {ECO:0000255|HAMAP-Rule:MF_01428}.
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DR   EMBL; AE017283; AAT83134.1; -; Genomic_DNA.
DR   RefSeq; WP_009640076.1; NC_006085.1.
DR   AlphaFoldDB; Q6A7Y1; -.
DR   SMR; Q6A7Y1; -.
DR   STRING; 267747.PPA1383; -.
DR   EnsemblBacteria; AAT83134; AAT83134; PPA1383.
DR   KEGG; pac:PPA1383; -.
DR   PATRIC; fig|267747.3.peg.1428; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_015768_0_0_11; -.
DR   OMA; WLLRMED; -.
DR   Proteomes; UP000000603; Chromosome.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01428; Glu_Q_tRNA_synth; 1.
DR   InterPro; IPR022380; Glu-Q_tRNA(Asp)_Synthase.
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; Zinc.
FT   CHAIN           1..347
FT                   /note="Glutamyl-Q tRNA(Asp) synthetase"
FT                   /id="PRO_0000208313"
FT   MOTIF           34..44
FT                   /note="'HIGH' region"
FT   MOTIF           259..263
FT                   /note="'KMSKS' region"
FT   BINDING         31..35
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         67
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         203
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         221
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         262
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
SQ   SEQUENCE   347 AA;  37357 MW;  3B86F6E74E0D9F7D CRC64;
     MPAASPQLLP TLPLVTDFAT THSGLRHAAG RFAPSPTSAL HLGNLRTALA AWLLARSTGR
     RFVVRIEDLD RARVAAAGKI ASTQLRDLES LGLDWDGPVV RQSERLDLYA DAVAGLETYP
     CFCTRREIAA ATTAPNEADW RPYPGTCRRL TVQQRHERLT TRAPATRLAS QLNTFEATDL
     ARGCARGRVD DLVLVRNDGT PAYNLAVVVD DGLQGVDQVV RARDLWSSAP RQAQLAELLG
     FIPPVYAHTG LVTGPGGVRL SKSAGAAGLS DLVDSGIDHR QVVAWLCRSL GLPEVADPHE
     LVNNVALTPP TPVAGIHRLD PRPLGGAMGW WSDAVLDVAV LRETRRP