ID A0A0G0N044_9BACT Unreviewed; 350 AA.
AC A0A0G0N044;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 32.
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=US90_C0006G0039 {ECO:0000313|EMBL:KKQ70486.1};
OS Candidatus Shapirobacteria bacterium GW2011_GWE2_38_30.
OC Bacteria; Candidatus Shapirobacteria.
OX NCBI_TaxID=1618490 {ECO:0000313|EMBL:KKQ70486.1, ECO:0000313|Proteomes:UP000034406};
RN [1] {ECO:0000313|EMBL:KKQ70486.1, ECO:0000313|Proteomes:UP000034406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKQ70486.1}.
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DR EMBL; LBUT01000006; KKQ70486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0N044; -.
DR STRING; 1618490.US90_C0006G0039; -.
DR PATRIC; fig|1618490.4.peg.303; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000034406; Unassembled WGS sequence.
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:KKQ70486.1};
KW Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW Rule:MF_00113};
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 350 AA; 39703 MW; DAAE08F4C16482F5 CRC64;
MLNPTDFDYH LPKNQIANQP LNNRDQSRLL FVDRSSQKLS DHHFFEIENY LGKNDVLVLN
QTKVFPARIF GQKSTGGHFE ILLAHQISQD TLEALSRPRL KSGLLLNFSS LLSAQIIDSN
PDTGLITLKF NQFGTEFYQS LNQLGHTPIP PYIKNSQSEK ILRQNYQTIY AKNTGSSAAP
TAGLHFTKEL LKKLSDRGVQ IEYVTLHVGL GTFQPLRLEN LKSKTLHTES YFIDPDTINR
LNNAKKSGKK ITAVGTTTTR CLESFAINPT ATSTQLFIYP PYKFKFVDSL ITNFHLPQSS
LLMLVYAFCS HPNTPQKFSI FSDSLIGQAY LYAVQNDYRF FSFGDAMWII
//
