ID   QUEA_SALTY              Reviewed;         354 AA.
AC   Q8ZRD9;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=STM0404;
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: 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}.
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DR   EMBL; AE006468; AAL19358.1; -; Genomic_DNA.
DR   RefSeq; NP_459399.1; NC_003197.2.
DR   RefSeq; WP_001266530.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZRD9; -.
DR   SMR; Q8ZRD9; -.
DR   STRING; 99287.STM0404; -.
DR   PaxDb; Q8ZRD9; -.
DR   EnsemblBacteria; AAL19358; AAL19358; STM0404.
DR   GeneID; 1251923; -.
DR   KEGG; stm:STM0404; -.
DR   PATRIC; fig|99287.12.peg.431; -.
DR   HOGENOM; CLU_039110_1_0_6; -.
DR   OMA; YSYGDGM; -.
DR   PhylomeDB; Q8ZRD9; -.
DR   BioCyc; SENT99287:STM0404-MON; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051075; F:S-adenosylmethionine:tRNA ribosyltransferase-isomerase activity; IBA:GO_Central.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0002099; P:tRNA wobble guanine modification; IBA:GO_Central.
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;
KW   Cytoplasm; Queuosine biosynthesis; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..354
FT                   /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT                   isomerase"
FT                   /id="PRO_0000165435"
SQ   SEQUENCE   354 AA;  39256 MW;  70EEAC90F135E959 CRC64;
     MRVTDFSFEL PESLIAHYPQ PERSRCRLLS LEGPTGALTH GTFTDLLDKL NPGDLLVFNN
     TRVIPARLFG RKASGGKIEV LVERMLDDKR ILAHIRASKA PKPGTELLLG DDESIHATMT
     ARHGALFEVE FNDPRPVLDI LNAIGHMPLP PYIDRPDEDA DRELYQTVYS EKPGAVAAPT
     AGLHFDEPLL AALREKGVEM AFVTLHVGAG TFQPVRVDTI EDHIMHSEYA EVPQEVVDAV
     LAAKARGNRV IAVGTTSVRS LESAAQAAKS DLIEPFFGDT QIFIYPGYQY KVIDALITNF
     HLPESTLIML VSAFAGYQHT MNAYKTAVEQ KYRFFSYGDA MFITYNPQAI SERP