(data stored in SCRATCH zone)

SWISSPROT: C8U1L4_ECO10

ID   C8U1L4_ECO10            Unreviewed;       308 AA.
AC   C8U1L4;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   RecName: Full=Glutamyl-Q tRNA(Asp) synthetase {ECO:0000256|HAMAP-Rule:MF_01428, ECO:0000256|SAAS:SAAS00346794};
DE            Short=Glu-Q-RSs {ECO:0000256|HAMAP-Rule:MF_01428};
DE            EC=6.1.1.- {ECO:0000256|HAMAP-Rule:MF_01428, ECO:0000256|SAAS:SAAS00346799};
GN   Name=yadB {ECO:0000313|EMBL:BAI29022.1};
GN   Synonyms=gluQ {ECO:0000256|HAMAP-Rule:MF_01428};
GN   OrderedLocusNames=ECO103_0144 {ECO:0000313|EMBL:BAI29022.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29022.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29022.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Catalyzes the tRNA-independent activation of glutamate
CC       in presence of ATP and the subsequent transfer of glutamate onto a
CC       tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-
CC       dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the
CC       wobble position of the QUC anticodon. {ECO:0000256|HAMAP-
CC       Rule:MF_01428}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01428};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01428};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. GluQ subfamily. {ECO:0000256|HAMAP-Rule:MF_01428,
CC       ECO:0000256|SAAS:SAAS00542009}.
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DR   EMBL; AP010958; BAI29022.1; -; Genomic_DNA.
DR   RefSeq; WP_000937424.1; NC_013353.1.
DR   SMR; C8U1L4; -.
DR   EnsemblBacteria; BAI29022; BAI29022; ECO103_0144.
DR   KEGG; eoh:ECO103_0144; -.
DR   HOGENOM; HOG000252723; -.
DR   KO; K01894; -.
DR   OMA; WLLRMED; -.
DR   BioCyc; ECOL585395:ECO103_RS00735-MONOMER; -.
DR   Proteomes; UP000000959; 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:0006412; P:translation; IEA:UniProtKB-KW.
DR   GO; GO:0043039; P:tRNA aminoacylation; IEA:InterPro.
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; C8U1L4.
DR   SWISS-2DPAGE; C8U1L4.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01428,
KW   ECO:0000256|RuleBase:RU363037, ECO:0000256|SAAS:SAAS00315323};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01428,
KW   ECO:0000256|RuleBase:RU363037, ECO:0000256|SAAS:SAAS00315316};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01428,
KW   ECO:0000256|RuleBase:RU363037, ECO:0000256|SAAS:SAAS00315306};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01428,
KW   ECO:0000256|SAAS:SAAS00315314};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01428,
KW   ECO:0000256|RuleBase:RU363037, ECO:0000256|SAAS:SAAS00315320};
KW   Protein biosynthesis {ECO:0000256|RuleBase:RU363037};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01428, ECO:0000256|SAAS:SAAS00315315}.
FT   DOMAIN       19    284       tRNA-synt_1c. {ECO:0000259|Pfam:PF00749}.
FT   REGION       19     23       Glutamate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01428}.
FT   MOTIF        22     32       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_01428}.
FT   MOTIF       238    242       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_01428}.
FT   METAL       111    111       Zinc. {ECO:0000256|HAMAP-Rule:MF_01428}.
FT   METAL       113    113       Zinc. {ECO:0000256|HAMAP-Rule:MF_01428}.
FT   METAL       125    125       Zinc. {ECO:0000256|HAMAP-Rule:MF_01428}.
FT   METAL       129    129       Zinc. {ECO:0000256|HAMAP-Rule:MF_01428}.
FT   BINDING      55     55       Glutamate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01428}.
FT   BINDING     182    182       Glutamate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01428}.
FT   BINDING     200    200       Glutamate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01428}.
FT   BINDING     241    241       ATP. {ECO:0000256|HAMAP-Rule:MF_01428}.
SQ   SEQUENCE   308 AA;  34868 MW;  69BA4A164AB4363C CRC64;
     MLPPYFLFKE MTDTQYIGRF APSPSGELHF GSLIAALGSY LQARARQGRW LVRIEDIDPP
     REVPGAAETI LRQLEHYGLH WDGDVLWQSQ RHDAYREALA WLHEQGLSYY CTCTRARIQS
     IGGIYDGHCR VLHHGPDNAA VRIRQQHPVT QFTDQLRGII HADEKLARED FIIHRRDGLF
     AYNLAVVVDD HFQGVTEIVR GADLIEPTVR QISLYQLFGW KVPDYIHLPL ALNPQGAKLS
     KQNHAPALPK GDPRPVLIAA LQFLGQQAEA HWQDFSVEQI LQSAVKNWRL TAVPESAIVN
     STFSNASC
//

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