ID A0A1M6TDJ7_9AQUI Unreviewed; 334 AA.
AC A0A1M6TDJ7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=S-adenosylmethionine:tRNA ribosyltransferase-isomerase {ECO:0000256|HAMAP-Rule:MF_00113};
DE EC=2.4.99.17 {ECO:0000256|HAMAP-Rule:MF_00113};
DE AltName: Full=Queuosine biosynthesis protein QueA {ECO:0000256|HAMAP-Rule:MF_00113};
GN Name=queA {ECO:0000256|HAMAP-Rule:MF_00113};
GN ORFNames=SAMN05444391_1407 {ECO:0000313|EMBL:SHK54959.1};
OS Thermocrinis minervae.
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Thermocrinis.
OX NCBI_TaxID=381751 {ECO:0000313|EMBL:SHK54959.1, ECO:0000313|Proteomes:UP000189810};
RN [1] {ECO:0000313|EMBL:SHK54959.1, ECO:0000313|Proteomes:UP000189810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19557 {ECO:0000313|EMBL:SHK54959.1,
RC ECO:0000313|Proteomes:UP000189810};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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:0000256|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 + 2 H(+) + L-
CC methionine; Xref=Rhea:RHEA:32155, Rhea:RHEA-COMP:10342, Rhea:RHEA-
CC COMP:18582, ChEBI:CHEBI:15378, ChEBI:CHEBI:16708, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:82833, ChEBI:CHEBI:194443;
CC EC=2.4.99.17; Evidence={ECO:0000256|HAMAP-Rule:MF_00113};
CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00113}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00113}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00113}.
CC -!- SIMILARITY: Belongs to the QueA family. {ECO:0000256|HAMAP-
CC Rule:MF_00113}.
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DR EMBL; LT670846; SHK54959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6TDJ7; -.
DR STRING; 381751.SAMN05444391_1407; -.
DR OrthoDB; 9805933at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000189810; Chromosome i.
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; QueA-like; 1.
DR Gene3D; 3.40.1780.10; QueA-like; 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 NCBIfam; TIGR00113; queA; 1.
DR PANTHER; PTHR30307; S-ADENOSYLMETHIONINE:TRNA RIBOSYLTRANSFERASE-ISOMERASE; 1.
DR PANTHER; PTHR30307:SF0; S-ADENOSYLMETHIONINE:TRNA RIBOSYLTRANSFERASE-ISOMERASE; 1.
DR Pfam; PF02547; Queuosine_synth; 1.
DR SUPFAM; SSF111337; QueA-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00113};
KW Isomerase {ECO:0000313|EMBL:SHK54959.1};
KW Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW Rule:MF_00113}; Reference proteome {ECO:0000313|Proteomes:UP000189810};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00113};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00113}.
SQ SEQUENCE 334 AA; 38243 MW; B48F95DA0DBBCA43 CRC64;
MRVEEFDYYL PLELIAKYPV EPRHAARLMV VRRDTGDITH STFWNLDEFL EEGDLLVFNN
SKVLPARLKA FKSTGGKVEV LLTDYITKDT WQALVGGKNI KEGMTLKVSE DFKVEVLKHI
EGPKFLVKLV AEDPLKALDK YGRIPIPPYL EREDEPIDRI YYQTVFAREE GSVAAPTASL
HFSEELLQKL QNKGIKMAFI TLHVSYGTFK PVKVERVEEH RVDPEYIKVP QETVEAILQT
KQKGKRVVAV GTTTVRALET AGFKPYEGWT DLYIYPGYSF RVVDALITNF HLPKSSLLFL
VCSFGGKDLI MKAYKIAVEN RYRFYSYGDG MLIL
//
