QUEA_BACFR
ID QUEA_BACFR Reviewed; 352 AA.
AC Q650L7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=BF0058;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD46807.1; -; Genomic_DNA.
DR RefSeq; WP_005783637.1; NZ_UYXF01000012.1.
DR RefSeq; YP_097341.1; NC_006347.1.
DR AlphaFoldDB; Q650L7; -.
DR SMR; Q650L7; -.
DR STRING; 295405.BF0058; -.
DR PRIDE; Q650L7; -.
DR EnsemblBacteria; BAD46807; BAD46807; BF0058.
DR GeneID; 66330802; -.
DR KEGG; bfr:BF0058; -.
DR PATRIC; fig|295405.11.peg.96; -.
DR HOGENOM; CLU_039110_1_0_10; -.
DR OMA; LSKHKMD; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000002197; 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; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..352
FT /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT isomerase"
FT /id="PRO_0000231318"
SQ SEQUENCE 352 AA; 40464 MW; 4B1B6CE480990378 CRC64;
MKLSQFKFKL PEEKIALHPT KYRDESRLMV LHKRTGEIEH KMFKDILNYF DDKDVFVFND
TKVFPARLYG NKEKTGARIE VFLLRELNEE LRLWDVLVDP ARKIRIGNKL YFGDDDSMVA
EVIDNTTSRG RTLRFLYDGP HDEFKKALYA LGETPLPHTI LNRPVEEEDA ERFQSIFAKN
EGAVTAPTAS LHFSRELMKR MEIKGIDFAY ITLHAGLGNF RDIDVEDLTK HKMDSEQMFV
TEEAVKIVNR AKDLGKNVCA VGTTVMRAIE STVSTDGHLK EYEGWTNKFI FPPYDFTVAN
AMVSNFHMPL STLLMIVAAF GGYDQVMDAY HIALKEGYRF GTYGDAMLIL DK
