ID A0A1B3LJN8_9PROT Unreviewed; 354 AA.
AC A0A1B3LJN8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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 ECO:0000313|EMBL:AOF81065.1};
GN ORFNames=BSY238_913 {ECO:0000313|EMBL:AOF81065.1};
OS Methyloversatilis sp. RAC08.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sterolibacteriaceae; Methyloversatilis.
OX NCBI_TaxID=1842540 {ECO:0000313|EMBL:AOF81065.1, ECO:0000313|Proteomes:UP000094168};
RN [1] {ECO:0000313|Proteomes:UP000094168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RAC08 {ECO:0000313|Proteomes:UP000094168};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-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; CP016448; AOF81065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B3LJN8; -.
DR STRING; 1842540.BSY238_913; -.
DR KEGG; metr:BSY238_913; -.
DR PATRIC; fig|1842540.3.peg.919; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000094168; 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; 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 Glycosyltransferase {ECO:0000313|EMBL:AOF81065.1};
KW Isomerase {ECO:0000313|EMBL:AOF81065.1};
KW Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW Rule:MF_00113}; Reference proteome {ECO:0000313|Proteomes:UP000094168};
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 354 AA; 38762 MW; A11521EBCD0461E6 CRC64;
MPHSVLTLSD FDYDLPDDLI AQAPLPERSA SRLLVVGTTS LTDSSIRALP QWLEPDDLLV
FNDTRVMHAR LYGTKSSGGR IEVLIERLTG EHEALAQVRA SKTPRAGSRL RMEDAFDFEV
LGRDGEFFRL RSTDAAPLAA LLERHGRLPL PPYIERAAAD ADEQRYQTVY ARQTGSVAAP
TAGLHFDDAL LEAVAARGVR QAHVTLHVGA GTFQPVRTDN LAEHRMHSEQ FQLPVDTAQA
IADTKASGGR VIAVGTTSLR CLESAAATCA PDPLAACQGD TRLFITPGYD FRVIDGLLTN
FHLPKSTLLM LVSALAGQQR VRAAYAHAVA QRYRFFSYGD AMFIPARMKD HDEV
//