QUEA_AMOA5
ID QUEA_AMOA5 Reviewed; 348 AA.
AC B3ESF6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=S-adenosylmethionine:tRNA ribosyltransferase-isomerase {ECO:0000255|HAMAP-Rule:MF_00113};
DE EC=2.4.99.17 {ECO:0000255|HAMAP-Rule:MF_00113};
DE AltName: Full=Queuosine biosynthesis protein QueA {ECO:0000255|HAMAP-Rule:MF_00113};
GN Name=queA {ECO:0000255|HAMAP-Rule:MF_00113}; OrderedLocusNames=Aasi_0780;
OS Amoebophilus asiaticus (strain 5a2).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Amoebophilaceae;
OC Candidatus Amoebophilus.
OX NCBI_TaxID=452471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5a2;
RX PubMed=20023027; DOI=10.1128/jb.01379-09;
RA Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M.,
RA Rattei T., Horn M.;
RT "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus'
RT reveals common mechanisms for host cell interaction among amoeba-associated
RT bacteria.";
RL J. Bacteriol. 192:1045-1057(2010).
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:0000255|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 + H(+) + L-
CC methionine; Xref=Rhea:RHEA:32155, Rhea:RHEA-COMP:10342, Rhea:RHEA-
CC COMP:10346, ChEBI:CHEBI:15378, ChEBI:CHEBI:16708, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:82833, ChEBI:CHEBI:82834;
CC EC=2.4.99.17; Evidence={ECO:0000255|HAMAP-Rule:MF_00113};
CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00113}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00113}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00113}.
CC -!- SIMILARITY: Belongs to the QueA family. {ECO:0000255|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; CP001102; ACE06158.1; -; Genomic_DNA.
DR RefSeq; WP_012472927.1; NC_010830.1.
DR AlphaFoldDB; B3ESF6; -.
DR SMR; B3ESF6; -.
DR STRING; 452471.Aasi_0780; -.
DR EnsemblBacteria; ACE06158; ACE06158; Aasi_0780.
DR KEGG; aas:Aasi_0780; -.
DR eggNOG; COG0809; Bacteria.
DR HOGENOM; CLU_039110_1_0_10; -.
DR OMA; LSKHKMD; -.
DR OrthoDB; 368001at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000001227; 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; -; 1.
DR Gene3D; 3.40.1780.10; -; 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; PTHR30307; 1.
DR Pfam; PF02547; Queuosine_synth; 1.
DR SUPFAM; SSF111337; SSF111337; 1.
DR TIGRFAMs; TIGR00113; queA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Queuosine biosynthesis; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..348
FT /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT isomerase"
FT /id="PRO_1000117521"
SQ SEQUENCE 348 AA; 39393 MW; 848888ECDD5EAE06 CRC64;
MKLSSFKFTL PSKLIASHPV ENREDARLMV VHKRTGQIEH KTFKDLIDYL GENDTLVLND
AKIFPSKLYG SKEKTGAQIE VFLLRELESG EHLWDTLVEP ARKIRVGNKL YFGDGELVAE
VLDNTTSRGR TLKFLFEGTR EEFYEIVDQL GFVPLPNQLK RKPETEDRER YQTVYAQHIG
AVVPPFAGLH FSAHLLKRLE LKGVHITPLT LHIGLNSMKI IDVEDLTKYR IGSEQFLIPD
NTVTTVNTAL DDKKQVCAVG TSTIKALETS VSVAGRLKPA QGWTNKLIFP PYDFKVCTSL
ITNFHLPESL PLVNAAAFGG YELMMEAYQI AIKEKYRFFV YGDAMLII