GenomeNet

Database: UniProt
Entry: I2JN13_9GAMM
LinkDB: I2JN13_9GAMM
Original site: I2JN13_9GAMM 
ID   I2JN13_9GAMM            Unreviewed;       371 AA.
AC   I2JN13;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=DOK_03905 {ECO:0000313|EMBL:EIF44365.1};
OS   gamma proteobacterium BDW918.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Spongiibacteraceae.
OX   NCBI_TaxID=1168065 {ECO:0000313|EMBL:EIF44365.1, ECO:0000313|Proteomes:UP000003473};
RN   [1] {ECO:0000313|EMBL:EIF44365.1, ECO:0000313|Proteomes:UP000003473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BDW918 {ECO:0000313|EMBL:EIF44365.1,
RC   ECO:0000313|Proteomes:UP000003473};
RX   PubMed=22740675; DOI=10.1128/JB.00678-12;
RA   Kim S.M., Cho S.J., Lee S.B.;
RT   "Genome Sequence of the Unclassified Marine Gammaproteobacterium BDW918.";
RL   J. Bacteriol. 194:3753-3754(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}.
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:EIF44365.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJMK01000020; EIF44365.1; -; Genomic_DNA.
DR   AlphaFoldDB; I2JN13; -.
DR   PATRIC; fig|1168065.3.peg.823; -.
DR   eggNOG; COG0809; Bacteria.
DR   HOGENOM; CLU_039110_1_0_6; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000003473; 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:EIF44365.1};
KW   Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW   Rule:MF_00113}; Reference proteome {ECO:0000313|Proteomes:UP000003473};
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   371 AA;  41124 MW;  976909ECE199703F CRC64;
     MTNSANLAPF QMKADIMRRS DFNFELPESL IAYYPMPERD ASRLLVLNSQ QQCEHRQFKA
     LPDYLRAGDL LVFNNTRVIP ARLFATKESG GRIEILVERI VDEYRVLAHV RSSKSPKAGA
     TLWLAANNTD APGTESVAVL GRHDALFELE FAEPVLTVLS RLGHMPLPPY IEREDAAEDR
     ERYQTVYASR DGAVAAPTAG LHFTENLIQQ CVAKGVELAF VTLHVGAGTF QPVRADDIRD
     HQMHAEYIEV PEEVAEQVRA TRVRGGRVVA VGTTSVRSLE SASQSGEIAA FAGDSRIFIY
     PGYQFRSVDM MVTNFHLPES TLIMLVSAFA GQAAVLNAYR EAVAEQYRFF SYGDAMLVFP
     ATNTEITGNT V
//
DBGET integrated database retrieval system