ID   QUEA_BORBU              Reviewed;         343 AA.
AC   O51053; P70829;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   25-MAY-2022, entry version 107.
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=BB_0021;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-108.
RC   STRAIN=HB19;
RA   Boursaux-Eude C., Margarita D., Belfaiza J., Old I.G., Saint-Girons I.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AE000783; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE000783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Y08885; CAA70098.1; -; Genomic_DNA.
DR   PIR; E70102; E70102.
DR   AlphaFoldDB; O51053; -.
DR   SMR; O51053; -.
DR   PRIDE; O51053; -.
DR   OMA; LSKHKMD; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001807; 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..343
FT                   /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT                   isomerase"
FT                   /id="PRO_0000165382"
FT   CONFLICT        11
FT                   /note="S -> P (in Ref. 2; CAA70098)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        41
FT                   /note="K -> E (in Ref. 2; CAA70098)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        61
FT                   /note="A -> V (in Ref. 2; CAA70098)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68
FT                   /note="A -> V (in Ref. 2; CAA70098)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        85
FT                   /note="D -> G (in Ref. 2; CAA70098)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   343 AA;  39746 MW;  C505C7D6D6E131C5 CRC64;
     MKTKEFHFNL SHSLIEQYPS EKRGSSRLIV LDPQLQKIYH KNSVNNILKY INSNIFNNSK
     ARKSRIYAES EMSSNVEFLI LDRIDTNLFT ALVSKSKKQI IGNFYKFPEG LMDEILSKNS
     SEVVLKFNNN VGEDYFEKHC FVPLPSYIKR DYDKIDEDRY QTIYSKYVGS TASATAGLHF
     SRDLFSAFEN NNIEYDFITL HVGAGTFLPV RSKKVEEHNM HFETFLIKDF VAVRLQNAKL
     LGKRILSIVT TTLRALESSY DNNLKKFKTG QQSTNLFIYP GKNYCFKFVD MLFTNFHTPQ
     STLLMLVSSF AGKDFVFSFY EEAINKGYKF FSYGDAMLIL NNI