QUEA_RICAH
ID QUEA_RICAH Reviewed; 371 AA.
AC A8GMK3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=A1C_01585;
OS Rickettsia akari (strain Hartford).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=293614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hartford;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia akari.";
RL Submitted (SEP-2007) 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: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}.
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DR EMBL; CP000847; ABV74628.1; -; Genomic_DNA.
DR RefSeq; WP_012149262.1; NC_009881.1.
DR AlphaFoldDB; A8GMK3; -.
DR SMR; A8GMK3; -.
DR STRING; 293614.A1C_01585; -.
DR EnsemblBacteria; ABV74628; ABV74628; A1C_01585.
DR KEGG; rak:A1C_01585; -.
DR eggNOG; COG0809; Bacteria.
DR HOGENOM; CLU_039110_1_0_5; -.
DR OMA; YSYGDGM; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000006830; 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; 2.
DR Pfam; PF02547; Queuosine_synth; 1.
DR SUPFAM; SSF111337; SSF111337; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Queuosine biosynthesis; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..371
FT /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT isomerase"
FT /id="PRO_1000015260"
SQ SEQUENCE 371 AA; 42779 MW; C7BFDD97C91225A4 CRC64;
MKLSAFDFNL PSELIAQSPS SERDNSDLLI AAMPPIKTKF YNIIDYLKEG DLLVLNNSKV
IKAKLHLWKN VTINLNQKLS DDSWSAFAKP TRKLHVNDEF YFDNHKVIIT EKLVMGEIKV
KFDLDNISVF EFLDKYGEMP LPVYIRRSHS LYHTTSTLCH TRENGYSEKL DAFFRRNDIK
DKDNDIVYDN ERYQTIYSQI EGSVAAPTAG LHFTNDILDK LKTKGIHTAF LTLHVGAGTF
LPVKTENIHE HKMHTEYCSI TPETAEIINK AKQERRRIIA VGTTTLRTVE SFCNNGIIKA
GSFETDIFIT PGFKFQTADM LLTNFHFPKS TLFMLICAFA GFKEMHELYK YAIKEKMRFF
SYGDATLLYR K