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Database: UniProt
Entry: G8X5B5_FLACA
LinkDB: G8X5B5_FLACA
Original site: G8X5B5_FLACA 
ID   G8X5B5_FLACA            Unreviewed;       349 AA.
AC   G8X5B5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
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:AEW85526.1};
GN   OrderedLocusNames=FCOL_03420 {ECO:0000313|EMBL:AEW85526.1};
OS   Flavobacterium columnare (strain ATCC 49512 / CIP 103533 / TG 44/87).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1041826 {ECO:0000313|EMBL:AEW85526.1, ECO:0000313|Proteomes:UP000005638};
RN   [1] {ECO:0000313|Proteomes:UP000005638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49512 / CIP 103533 / TG 44/87
RC   {ECO:0000313|Proteomes:UP000005638};
RA   Tekedar H.C., Karsi A., Gillaspy A.F., Dyer D., Benton N.R., Zaitshik J.,
RA   Vamenta S., Banes M.M., Gulsoy N., Aboko-Cole M., Waldbieser G.C.,
RA   Lawrence M.L.;
RT   "Complete genome sequence of Flavobacterium columnare ATCC 49512.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEW85526.1, ECO:0000313|Proteomes:UP000005638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49512 / CIP 103533 / TG 44/87
RC   {ECO:0000313|Proteomes:UP000005638};
RX   PubMed=22535941; DOI=10.1128/JB.00281-12;
RA   Tekedar H.C., Karsi A., Gillaspy A.F., Dyer D.W., Benton N.R., Zaitshik J.,
RA   Vamenta S., Banes M.M., Gulsoy N., Aboko-Cole M., Waldbieser G.C.,
RA   Lawrence M.L.;
RT   "Genome Sequence of the Fish Pathogen Flavobacterium columnare ATCC
RT   49512.";
RL   J. Bacteriol. 194:2763-2764(2012).
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; CP003222; AEW85526.1; -; Genomic_DNA.
DR   RefSeq; WP_014164809.1; NC_016510.2.
DR   AlphaFoldDB; G8X5B5; -.
DR   STRING; 1041826.FCOL_03420; -.
DR   GeneID; 60759144; -.
DR   KEGG; fco:FCOL_03420; -.
DR   eggNOG; COG0809; Bacteria.
DR   HOGENOM; CLU_039110_1_0_10; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000005638; 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   Isomerase {ECO:0000313|EMBL:AEW85526.1};
KW   Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW   Rule:MF_00113}; Reference proteome {ECO:0000313|Proteomes:UP000005638};
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   349 AA;  40017 MW;  A52C58BF584C71D4 CRC64;
     MKLSNFNFNL PAELLAEYPA ENRDESRLMV VHRKTGEIEH KLFKDIIEYF DEGDVMVVNN
     TKVFPARLYG NKEKTGARIE VFLLRELNAE QRLWDVLVDP ARKIRIGNKL YFGDDDSLVA
     EVIDNTTSRG RTLRFLYDGS YEEFRQKLVD LGETPIPKYI NREVTEEDAE RYQTIYAKEE
     GAVAAPTAGL HFSKHLMKRL EIKGINFAEV TLHVGLGTFN PVEVEDLSKH KMDSEEVLIS
     DEACETVNKA KLNKKRVCAI GTTTMRAMES SVSSNKTLNS YQGWTNKFIF PPYDFSVADC
     MVTNFHTPKS TLLMMISAFC GHDLMMKAYK EAVEQKYRFY SYGDAMLIL
//
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