ID   QUEA_SYNWW              Reviewed;         352 AA.
AC   Q0AX18;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=Swol_1429;
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen;
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000448; ABI68736.1; -; Genomic_DNA.
DR   RefSeq; WP_011640835.1; NC_008346.1.
DR   AlphaFoldDB; Q0AX18; -.
DR   SMR; Q0AX18; -.
DR   STRING; 335541.Swol_1429; -.
DR   EnsemblBacteria; ABI68736; ABI68736; Swol_1429.
DR   KEGG; swo:Swol_1429; -.
DR   eggNOG; COG0809; Bacteria.
DR   HOGENOM; CLU_039110_1_0_9; -.
DR   OMA; YSYGDGM; -.
DR   OrthoDB; 368001at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001968; 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..352
FT                   /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT                   isomerase"
FT                   /id="PRO_1000057744"
SQ   SEQUENCE   352 AA;  39873 MW;  2ECC94F5F15E428B CRC64;
     MQHDKNEDIY RLSTYYYDLP PELIAQYPAE YRDSSRLLVL DRKSGDLNDR AFKDISLYLK
     KGDALVLNET RVIPARFFAY KESGARVEIL LLKKLGDDWE ALVKPARRLK AGSRVFLSPD
     KPLVIEIVEE LDFAGGRRVR FQDSVDEDTL LQEQGHIPLP PYINRPDEEL DRERYQTVYA
     CKSGSVAAPT AGLHFTPDLL KEITLQGINI VRIVLHVGMG TFRPVKNEDI RQHNMHLEYY
     EVAEDAAALL NLTRESGGQI VAVGTTVVRT LESVYNKDCG FLAGKGETNK YIFPGYQFRA
     IDKLLTNFHL PGSSLLMLVA GFAGTESTLA AYRHAVENRY RFFSYGDAML VI