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Database: UniProt
Entry: A0A1V4M8Y8_9FIRM
LinkDB: A0A1V4M8Y8_9FIRM
Original site: A0A1V4M8Y8_9FIRM 
ID   A0A1V4M8Y8_9FIRM        Unreviewed;       344 AA.
AC   A0A1V4M8Y8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=AVO34_09125 {ECO:0000313|EMBL:OPL11188.1};
OS   Firmicutes bacterium ML8_F2.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1775675 {ECO:0000313|EMBL:OPL11188.1, ECO:0000313|Proteomes:UP000189969};
RN   [1] {ECO:0000313|EMBL:OPL11188.1, ECO:0000313|Proteomes:UP000189969}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ML8_F2 {ECO:0000313|EMBL:OPL11188.1};
RA   Hamilton T.L., Pearson A., Macalady J.;
RT   "Carbon and sulfur cycling below the chemocline in a meromictic lake.";
RL   Submitted (DEC-2015) 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}.
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:OPL11188.1}.
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DR   EMBL; LQBG01000066; OPL11188.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4M8Y8; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000189969; 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:OPL11188.1};
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   344 AA;  39242 MW;  8ADB91685F6D23B5 CRC64;
     MVEYKLSDYD YHLPIELIAQ EPLAERDKSR MMILEKRTGQ ITNSIFNRIP TYLKQGDLLV
     LNDTKVLPVR LLGQIVGKDT AVEILLLHRC RDERWIAMVR PGRKLKPGIK VSLEEDVTAL
     IEDYADKGLR EISFSVREPI EKLLPRLGRV PLPPYIKKEL SDPDQYQTIF AAREGSAAAP
     TAGFHFTDRV FAELDKKGVE KTFITLHIGP GTFQPVKEDD IREHVMHREY YQLHKSTVKA
     LNAARERGGR IVAVGTSVCR VLETVAESNG YFAGEAEGWT DLYIYPGYKF RAVNTLLTNF
     HLPRSTLLML VSAFAERKNI LYAYREAVAG QYRFFSFGDC MLII
//
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