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Database: UniProt
Entry: Q07Y01
LinkDB: Q07Y01
Original site: Q07Y01 
ID   GLUQ_SHEFN              Reviewed;         293 AA.
AC   Q07Y01;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 98.
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=Sfri_3277;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000447; ABI73113.1; -; Genomic_DNA.
DR   RefSeq; WP_011638716.1; NC_008345.1.
DR   AlphaFoldDB; Q07Y01; -.
DR   SMR; Q07Y01; -.
DR   STRING; 318167.Sfri_3277; -.
DR   KEGG; sfr:Sfri_3277; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_015768_0_1_6; -.
DR   OMA; WLLRMED; -.
DR   OrthoDB; 9807503at2; -.
DR   Proteomes; UP000000684; 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; HUPs; 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   NCBIfam; TIGR03838; queuosine_YadB; 1.
DR   PANTHER; PTHR43311; GLUTAMATE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43311:SF1; GLUTAMYL-Q TRNA(ASP) SYNTHETASE; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 2.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Zinc.
FT   CHAIN           1..293
FT                   /note="Glutamyl-Q tRNA(Asp) synthetase"
FT                   /id="PRO_1000024368"
FT   MOTIF           12..22
FT                   /note="'HIGH' region"
FT   MOTIF           228..232
FT                   /note="'KMSKS' region"
FT   BINDING         9..13
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         45
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         172
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         190
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
SQ   SEQUENCE   293 AA;  32687 MW;  DC7C2ED5F937029F CRC64;
     MIPPSYIGRF APSPSGSLHF GSLVAALGSY LRAHSQQGQW LVRIEDIDPP REVPGASDNI
     LRTLDAYGLH WHGTVLFQQQ RYQVYQDQIE AFIASDLAYY CQCTRKIIQT SGGVYDGRCG
     RLQPRLTHGA IRIRNHVKVD HFVDKLQGPV VVDKAFAEED FIIKRSDGLY AYQLAVVLDD
     AYQGITEVVR GCDLLEASCR QISLFTQLEF TPPDWLHLPL VCAEKGFKLS KQNYAPAIDV
     IHPQASINAA LTFLGQKAVD VDSVEVMLKQ AVEQFDLSTI PAQKEIVLST IND
//
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