QUEA_FRATF
ID QUEA_FRATF Reviewed; 338 AA.
AC A7NB92;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=FTA_0769;
OS Francisella tularensis subsp. holarctica (strain FTNF002-00 / FTA).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=458234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FTNF002-00 / FTA;
RX PubMed=19756146; DOI=10.1371/journal.pone.0007041;
RA Barabote R.D., Xie G., Brettin T.S., Hinrichs S.H., Fey P.D., Jay J.J.,
RA Engle J.L., Godbole S.D., Noronha J.M., Scheuermann R.H., Zhou L.W.,
RA Lion C., Dempsey M.P.;
RT "Complete genome sequence of Francisella tularensis subspecies holarctica
RT FTNF002-00.";
RL PLoS ONE 4:E7041-E7041(2009).
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; CP000803; ABU61245.1; -; Genomic_DNA.
DR RefSeq; WP_010030758.1; NC_009749.1.
DR AlphaFoldDB; A7NB92; -.
DR SMR; A7NB92; -.
DR KEGG; fta:FTA_0769; -.
DR HOGENOM; CLU_039110_1_0_6; -.
DR OMA; YSYGDGM; -.
DR UniPathway; UPA00392; -.
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..338
FT /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT isomerase"
FT /id="PRO_1000057742"
SQ SEQUENCE 338 AA; 38358 MW; DFD941ECB6D36D32 CRC64;
MKTDDFDYKL PEELIASYPL ENRDASRLLK LNKQTGEIAD YKFTDFIDFI NPGDLLVFNN
SKVMLARLYG SKTTGAKLEY LIERIKNPKL FETHIKANRS PAIGSEIYVE DTLAKVLDKD
GGMYLLEIQG DKDIYQLMEE FGHIPLPPYM KRDDEEFDAE RYQTVYAQDL GSVAALTAGL
HFSKELMQQI KDKGVDIAYI TLHVGSGTFK PVQVDDVESH KMHAEVISVP VEVCQKIRQT
KENGGRVITI GTTSVRSLET AGQNGQIEPY QGETDIFLYP GKKFNVVDAM ITNFHLPKST
LIMLVSAFAD KEKIIKAYEH AIAERYRFFS YGDAMFIF