GenomeNet

Database: UniProt
Entry: F7XY23_MOREP
LinkDB: F7XY23_MOREP
Original site: F7XY23_MOREP 
ID   F7XY23_MOREP            Unreviewed;       356 AA.
AC   F7XY23;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
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:AEI74999.1};
GN   OrderedLocusNames=MEPCIT_372 {ECO:0000313|EMBL:AEI74999.1};
OS   Moranella endobia (strain PCIT).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Candidatus Moranella.
OX   NCBI_TaxID=903503 {ECO:0000313|EMBL:AEI74999.1, ECO:0000313|Proteomes:UP000000504};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PCIT;
RA   McCutcheon J.P., von Dohlen C.D.;
RT   "An interdependent metabolic patchwork in the nested three-way symbiosis of
RT   mealybugs.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEI74999.1, ECO:0000313|Proteomes:UP000000504}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCIT {ECO:0000313|EMBL:AEI74999.1,
RC   ECO:0000313|Proteomes:UP000000504};
RX   PubMed=21835622; DOI=10.1016/j.cub.2011.06.051;
RA   McCutcheon J.P., von Dohlen C.D.;
RT   "An interdependent metabolic patchwork in the nested symbiosis of
RT   mealybugs.";
RL   Curr. Biol. 21:1366-1372(2011).
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   ---------------------------------------------------------------------------
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; CP002243; AEI74999.1; -; Genomic_DNA.
DR   RefSeq; WP_013975749.1; NC_015735.1.
DR   AlphaFoldDB; F7XY23; -.
DR   STRING; 903503.MEPCIT_372; -.
DR   KEGG; men:MEPCIT_372; -.
DR   eggNOG; COG0809; Bacteria.
DR   HOGENOM; CLU_039110_1_0_6; -.
DR   OMA; YSYGDGM; -.
DR   OrthoDB; 9805933at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000000504; 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:AEI74999.1};
KW   Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW   Rule:MF_00113}; Reference proteome {ECO:0000313|Proteomes:UP000000504};
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   356 AA;  39551 MW;  D571A428277C7415 CRC64;
     MRLDDFLFEL PAHLIARYPQ RERSACRLLS LDGETGALVH QVFTDLINNL APGDLLVFNN
     TRVIPARLFG RKISGGKIEI MVERIINDKQ VLAHVRASKV LKVGTTLLLG DDNSIAATMV
     ARHDSLYELR FNDQRDVLTL LDEKGHIPLP PYIDRPDNVA DSTRYQTVYS ERPGAVAAPT
     AGLHFDELIL AKLRAKGIEM AFVTLHVGAG TFQPVRVNRI EQHRMHSEYV EVPQEVVNAV
     LACKARAKRV VAVGTTSVRS LESAAAAAGE QVLAPFYGDT SIFIYPGYHF RVIDALITNF
     HLPKSTLIML VSAFAGYHHT VAAYREAVAQ EYRFFSYGDA MFITRNPTAA NIAHMN
//
DBGET integrated database retrieval system