ID   QUEA_ERWT9              Reviewed;         355 AA.
AC   B2VHQ4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=ETA_25400;
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
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; CU468135; CAO97586.1; -; Genomic_DNA.
DR   RefSeq; WP_012442251.1; NC_010694.1.
DR   AlphaFoldDB; B2VHQ4; -.
DR   SMR; B2VHQ4; -.
DR   STRING; 465817.ETA_25400; -.
DR   EnsemblBacteria; CAO97586; CAO97586; ETA_25400.
DR   KEGG; eta:ETA_25400; -.
DR   eggNOG; COG0809; Bacteria.
DR   HOGENOM; CLU_039110_1_0_6; -.
DR   OMA; YSYGDGM; -.
DR   OrthoDB; 368001at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001726; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051075; F:S-adenosylmethionine:tRNA ribosyltransferase-isomerase activity; IEA:UniProtKB-EC.
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;
KW   Cytoplasm; Queuosine biosynthesis; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..355
FT                   /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT                   isomerase"
FT                   /id="PRO_1000094775"
SQ   SEQUENCE   355 AA;  39139 MW;  3CD3E569BA78A989 CRC64;
     MRVADFTFEL PESLIAHYPQ AERSGCRLLS LNGSDGALTH GVFTDLLHKL NPGDLLVFNN
     TRVIPARIFG RKASGGKIEV LVERMLDDTR VLAHVRSSKA PKPGSDLLLG DDESVQATML
     ARHDTLFEIE FNDARPVLDI LNSIGHMPLP PYIDRPDEDA DRELYQTVYS QKPGAVAAPT
     AGLHFDEPLL VALREKGIET AFVTLHVGAG TFQPVRVDTI EDHIMHAEYA EVPQDVVDAV
     LACKARGNRV IAVGTTSVRS LESAAQAAEN TLIAPFFGDT KIFIYPGYHY QVIDALVTNF
     HLPESTLIML VSAFAGYKHT MRAYQQAVAE QYRFFSYGDA MFITRNPQAF AEIPG