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Database: UniProt
Entry: A0A0A2ETD5_PORCN
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ID   A0A0A2ETD5_PORCN        Unreviewed;       406 AA.
AC   A0A0A2ETD5;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=HQ35_07350 {ECO:0000313|EMBL:KGN79609.1}, SAMN02745205_01607
GN   {ECO:0000313|EMBL:SJZ68511.1};
OS   Porphyromonas cangingivalis.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=36874 {ECO:0000313|EMBL:KGN79609.1, ECO:0000313|Proteomes:UP000030125};
RN   [1] {ECO:0000313|EMBL:KGN79609.1, ECO:0000313|Proteomes:UP000030125}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COT-109 OH1386 {ECO:0000313|Proteomes:UP000030125}, and
RC   COT-109_OH1386 {ECO:0000313|EMBL:KGN79609.1};
RA   Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA   Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT   "Porphyromonas cangingivalis strain:COT-109_OH1386 Genome sequencing.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SJZ68511.1, ECO:0000313|Proteomes:UP000189956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700135 {ECO:0000313|EMBL:SJZ68511.1,
RC   ECO:0000313|Proteomes:UP000189956};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; JQJD01000048; KGN79609.1; -; Genomic_DNA.
DR   EMBL; FUWL01000014; SJZ68511.1; -; Genomic_DNA.
DR   RefSeq; WP_036852146.1; NZ_LR134506.1.
DR   AlphaFoldDB; A0A0A2ETD5; -.
DR   STRING; 36874.HQ34_09255; -.
DR   eggNOG; COG0809; Bacteria.
DR   OrthoDB; 9805933at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000030125; Unassembled WGS sequence.
DR   Proteomes; UP000189956; 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   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:SJZ68511.1};
KW   Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW   Rule:MF_00113}; Reference proteome {ECO:0000313|Proteomes:UP000030125};
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   406 AA;  45506 MW;  5AA57D7FF37B9BCC CRC64;
     MHDYKNTKIE SFSYHLPDER IAKYPLSRRD ESKLLRYSGG EITDHTFRDI SDIVEEDTLL
     VSNDTKVIRA RLEFFKPTGG RIEIFLLDPV APSVYETVFE ERSRCTWHCL VGNAKKWKED
     SITSTVTLPD GREIVLTATK ASPATPDGQE IALSWDGGAD FGAILEAYGE LPIPPYLNRE
     TEESDLTTYQ TLFARVQGSV AAPTAGLHFT PEVMQALSEK GIRSTQVTLH VGAGTFRPVK
     SETMEGHTMH TEAIVVSLET LKALKTHLGH ITAVGTTSTR TLESLYYIGV HLIEGKDSPF
     EVEQWEPYER DYKYSTEESL SAIIRHLEAS GEDHFVGATR IIIVPGFTFR LVGTLITNFH
     QPHSTLLLLI SAFVGNDWKS IYDHALANDY RFLSYGDSSI LFRPQA
//
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