(data stored in ACNUC7421 zone)

SWISSPROT: B7UII8_ECO27

ID   B7UII8_ECO27            Unreviewed;       308 AA.
AC   B7UII8;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 66.
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:CAS07695.1};
GN   Synonyms=gluQ {ECO:0000256|HAMAP-Rule:MF_01428};
GN   OrderedLocusNames=E2348C_0147 {ECO:0000313|EMBL:CAS07695.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07695.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07695.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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; FM180568; CAS07695.1; -; Genomic_DNA.
DR   RefSeq; WP_000937401.1; NC_011601.1.
DR   EnsemblBacteria; CAS07695; CAS07695; E2348C_0147.
DR   KEGG; ecg:E2348C_0147; -.
DR   HOGENOM; HOG000252723; -.
DR   KO; K01894; -.
DR   OMA; WLLRMED; -.
DR   BioCyc; ECOL574521:E2348C_RS00760-MONOMER; -.
DR   Proteomes; UP000008205; 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; B7UII8.
DR   SWISS-2DPAGE; B7UII8.
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:UP000008205};
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;  34898 MW;  C17BAEF1BFAD70E4 CRC64;
     MLPPYFLFKE MTDTHYIGRF APSPSGELHF GSLIAALGSY LQARARQGRW LVRIEDIDPP
     REVPGAAETI LRQLEHYGLH WDGDVLWQSQ RHHAYREALA WLHEQGLSYY CTCTRARIQS
     IGGIYDGHCR DLHHGPDNAA VRIRQQHPVT QFTDLLRGII HADEKLARED FIIHRRDGLF
     AYNLAVVVDD HFQGVSEIVR GADLIEPTVR QISLYQLFGW KVPDYIHLPL ALNPQGAKLS
     KQNHAPALPK GDPRPVLIAA LHFLGQQVET HWQDFSVEQI LQSAVKNWTL TAVPESAIVN
     STFSNASC
//

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