(data stored in SCRATCH3701 zone)

SWISSPROT: QUEA_ECOBW

ID   QUEA_ECOBW              Reviewed;         356 AA.
AC   C4ZTG2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   11-DEC-2019, entry version 54.
DE   RecName: Full=S-adenosylmethionine:tRNA ribosyltransferase-isomerase {ECO:0000255|HAMAP-Rule:MF_00113};
DE            EC=2.4.99.17 {ECO:0000255|HAMAP-Rule:MF_00113};
DE   AltName: Full=Queuosine biosynthesis protein QueA {ECO:0000255|HAMAP-Rule:MF_00113};
GN   Name=queA {ECO:0000255|HAMAP-Rule:MF_00113}; OrderedLocusNames=BWG_0287;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
CC   -!- FUNCTION: Transfers and isomerizes the ribose moiety from AdoMet to the
CC       7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give
CC       epoxyqueuosine (oQ-tRNA). {ECO:0000255|HAMAP-Rule:MF_00113}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-
CC         methionine = adenine + epoxyqueuosine(34) in tRNA + H(+) + L-
CC         methionine; Xref=Rhea:RHEA:32155, Rhea:RHEA-COMP:10342, Rhea:RHEA-
CC         COMP:10346, ChEBI:CHEBI:15378, ChEBI:CHEBI:16708, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:82833, ChEBI:CHEBI:82834;
CC         EC=2.4.99.17; Evidence={ECO:0000255|HAMAP-Rule:MF_00113};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00113}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00113}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00113}.
CC   -!- SIMILARITY: Belongs to the QueA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00113}.
DR   EMBL; CP001396; ACR65507.1; -; Genomic_DNA.
DR   RefSeq; WP_001266503.1; NC_012759.1.
DR   SMR; C4ZTG2; -.
DR   EnsemblBacteria; ACR65507; ACR65507; BWG_0287.
DR   KEGG; ebw:BWG_0287; -.
DR   HOGENOM; HOG000004401; -.
DR   KO; K07568; -.
DR   OMA; YSYGDGM; -.
DR   BioCyc; ECOL595496:BWG_RS01625-MONOMER; -.
DR   UniPathway; UPA00392; -.
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; C4ZTG2.
DR   SWISS-2DPAGE; C4ZTG2.
KW   Cytoplasm; Queuosine biosynthesis; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..356
FT                   /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT                   isomerase"
FT                   /id="PRO_1000202951"
SQ   SEQUENCE   356 AA;  39431 MW;  47F7F0090812DCF3 CRC64;
     MRVTDFSFEL PESLIAHYPM PERSSCRLLS LDGPTGALTH GTFTDLLDKL NPGDLLVFNN
     TRVIPARLFG RKASGGKIEV LVERMLDDKR ILAHIRASKA PKPGAELLLG DDESINATMT
     ARHGALFEVE FNDERSVLDI 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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