(data stored in SCRATCH zone)

SWISSPROT: C8U289_ECO10

ID   C8U289_ECO10            Unreviewed;       356 AA.
AC   C8U289;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   RecName: Full=S-adenosylmethionine:tRNA ribosyltransferase-isomerase {ECO:0000256|HAMAP-Rule:MF_00113, ECO:0000256|SAAS:SAAS00958187};
DE            EC=2.4.99.17 {ECO:0000256|HAMAP-Rule:MF_00113, ECO:0000256|SAAS:SAAS00958171};
DE   AltName: Full=Queuosine biosynthesis protein QueA {ECO:0000256|HAMAP-Rule:MF_00113};
GN   Name=queA {ECO:0000256|HAMAP-Rule:MF_00113,
GN   ECO:0000313|EMBL:BAI29247.1};
GN   OrderedLocusNames=ECO103_0379 {ECO:0000313|EMBL:BAI29247.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29247.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29247.1, 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: Transfers and isomerizes the ribose moiety from AdoMet
CC       to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give
CC       epoxyqueuosine (oQ-tRNA). {ECO:0000256|HAMAP-Rule:MF_00113,
CC       ECO:0000256|SAAS:SAAS00958175}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-
CC         L-methionine = adenine + epoxyqueuosine(34) in tRNA + H(+) + L-
CC         methionine; Xref=Rhea:RHEA:32155, Rhea:RHEA-COMP:10342,
CC         Rhea:RHEA-COMP:10346, ChEBI:CHEBI:15378, ChEBI:CHEBI:16708,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:82833,
CC         ChEBI:CHEBI:82834; EC=2.4.99.17; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00113, ECO:0000256|SAAS:SAAS01116098};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00113, ECO:0000256|SAAS:SAAS00958180}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00113,
CC       ECO:0000256|SAAS:SAAS00958162}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00113,
CC       ECO:0000256|SAAS:SAAS00958183}.
CC   -!- SIMILARITY: Belongs to the QueA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00113, ECO:0000256|SAAS:SAAS00958161}.
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DR   EMBL; AP010958; BAI29247.1; -; Genomic_DNA.
DR   RefSeq; WP_001266492.1; NC_013353.1.
DR   SMR; C8U289; -.
DR   EnsemblBacteria; BAI29247; BAI29247; ECO103_0379.
DR   KEGG; eoh:ECO103_0379; -.
DR   HOGENOM; HOG000004401; -.
DR   KO; K07568; -.
DR   OMA; YSYGDGM; -.
DR   BioCyc; ECOL585395:ECO103_RS01985-MONOMER; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.10.240; -; 1.
DR   Gene3D; 3.40.1780.10; -; 1.
DR   HAMAP; MF_00113; QueA; 1.
DR   InterPro; IPR003699; QueA.
DR   InterPro; IPR042118; QueA_dom1.
DR   InterPro; IPR042119; QueA_dom2.
DR   InterPro; IPR036100; QueA_sf.
DR   PANTHER; PTHR30307; PTHR30307; 1.
DR   Pfam; PF02547; Queuosine_synth; 1.
DR   SUPFAM; SSF111337; SSF111337; 1.
DR   TIGRFAMs; TIGR00113; queA; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U289.
DR   SWISS-2DPAGE; C8U289.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00113,
KW   ECO:0000256|SAAS:SAAS00958179};
KW   Isomerase {ECO:0000313|EMBL:BAI29247.1};
KW   Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00113,
KW   ECO:0000256|SAAS:SAAS00958170};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00113,
KW   ECO:0000256|SAAS:SAAS00958172};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00113,
KW   ECO:0000256|SAAS:SAAS00958166, ECO:0000313|EMBL:BAI29247.1}.
SQ   SEQUENCE   356 AA;  39417 MW;  A6B34E12E9ACC753 CRC64;
     MRVTDFSFEL PESLIAHYPM PERSSCRLLS LDGPTGALTH GTFTDLLDKL NPGDLLVFNN
     TRVIPARLFG RKASGGKIEV LVERMLDDKR ILAHIRASKA PKPGAELLLG DDESINATMT
     ARHGALFEVE FNDDRSVLDI LNSIGHMPLP PYIDRPDEDA DRELYQTVYS EKPGAVAAPT
     AGLHFDEPLL EKLRAKGVEM AFVTLHVGAG TFQPVRVDTI EDHIMHSEYA EVPQDVVDAV
     LAAKARGNRV IAVGTTSVRS LESAAQAAKN DLIEPFFDDT QIFIYPGFQY KVVDALVTNF
     HLPESTLIML VSAFAGYQHT MNAYKAAVEE KYRFFSYGDA MFITYNPQAI NERVGE
//

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