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QUEA_THET8
ID   QUEA_THET8              Reviewed;         345 AA.
AC   Q5SMH0;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=TTHA1058;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) 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}.
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DR   EMBL; AP008226; BAD70881.1; -; Genomic_DNA.
DR   RefSeq; WP_011173135.1; NC_006461.1.
DR   RefSeq; YP_144324.1; NC_006461.1.
DR   AlphaFoldDB; Q5SMH0; -.
DR   SMR; Q5SMH0; -.
DR   STRING; 300852.55772440; -.
DR   EnsemblBacteria; BAD70881; BAD70881; BAD70881.
DR   GeneID; 3169205; -.
DR   KEGG; ttj:TTHA1058; -.
DR   PATRIC; fig|300852.9.peg.1038; -.
DR   eggNOG; COG0809; Bacteria.
DR   HOGENOM; CLU_039110_1_1_0; -.
DR   OMA; YSYGDGM; -.
DR   PhylomeDB; Q5SMH0; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000000532; 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..345
FT                   /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT                   isomerase"
FT                   /id="PRO_0000231385"
SQ   SEQUENCE   345 AA;  38429 MW;  B4C220BF977366AD CRC64;
     MEGLEAYDYH LPPEQIAQEG VEPRDMARLM VVYREGPFRV AHKRVRDLPE FLRPGDVLVF
     NESKVIPARL LARKPTGGKV EILLVRERSP GLWEALLGPA RKAPPGTRLL LLSPKDLAPV
     PGLQAEVVAV EEDGVRLLRF QGDLVAHLEE VGEVPLPPYI KAKIPMERYQ TVYARRPGSV
     AAPTAGLHFT PELLERLREM GVELRFLTLH VGPGTFRPVK GDPEKHEMHA EPYAIPEEVA
     EAVNRAKAEG RRVVAVGTTV VRALESAYRE GVGVVAGEGE TRLFIRPPYT FKVVDALFTN
     FHLPRSTLLM LVAAFLGRER TLEAYRLAVA EGYRFYSLGD AMLIL
 
 
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