(data stored in ACNUC7421 zone)

SWISSPROT: GLUQ_SALTY

ID   GLUQ_SALTY              Reviewed;         298 AA.
AC   Q8ZRQ7;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   11-DEC-2019, entry version 105.
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=STM0185;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL19149.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE006468; AAL19149.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_459190.3; NC_003197.2.
DR   SMR; Q8ZRQ7; -.
DR   PaxDb; Q8ZRQ7; -.
DR   PRIDE; Q8ZRQ7; -.
DR   EnsemblBacteria; AAL19149; AAL19149; STM0185.
DR   GeneID; 1251703; -.
DR   KEGG; stm:STM0185; -.
DR   PATRIC; fig|99287.12.peg.195; -.
DR   eggNOG; ENOG4106F3G; Bacteria.
DR   eggNOG; COG0008; LUCA.
DR   HOGENOM; HOG000252723; -.
DR   KO; K01894; -.
DR   OMA; WLLRMED; -.
DR   PhylomeDB; Q8ZRQ7; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   Gene3D; 3.40.50.620; -; 2.
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.
DR   TIGRFAMs; TIGR03838; queuosine_YadB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8ZRQ7.
DR   SWISS-2DPAGE; Q8ZRQ7.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Zinc.
FT   CHAIN           1..298
FT                   /note="Glutamyl-Q tRNA(Asp) synthetase"
FT                   /id="PRO_0000208325"
FT   REGION          9..13
FT                   /note="Glutamate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   MOTIF           12..22
FT                   /note="'HIGH' region"
FT   MOTIF           228..232
FT                   /note="'KMSKS' region"
FT   METAL           101
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   METAL           103
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   METAL           115
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   METAL           119
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         45
FT                   /note="Glutamate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         172
FT                   /note="Glutamate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         190
FT                   /note="Glutamate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         231
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
SQ   SEQUENCE   298 AA;  33567 MW;  24A2A70C54F58276 CRC64;
     MTDSHYIGRF APSPSGELHF GSLIAALGSY LQARAQRGIW RVRIEDIDPP REVPGAAATI
     LRQLEHYGLH WDGEVLWQSQ RHEAYREALA WLHEQGLSYY CTCPRSRIQR LGGIYDGHCR
     TLCHGPENAA VRIKQQHPVM HFHDALRGDI QADPQLASED FIIHRRDGLF AYNLAVVVDD
     HFQGVTEIVR GADLIEPTVR QLSLYKQFGW RAPGYVHLPL ALNEQGAKLS KQNHAPALAT
     GDPRPVLVQA LRFLGQRDVV AWQEMSVEEL LRFAVAHWRL TAVPTSANVN PAFSNASR
//

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