QUEA_BRADU
ID QUEA_BRADU Reviewed; 366 AA.
AC Q89L59;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=bll4689;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC49954.1; -; Genomic_DNA.
DR RefSeq; NP_771329.1; NC_004463.1.
DR RefSeq; WP_011087458.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89L59; -.
DR SMR; Q89L59; -.
DR STRING; 224911.27352953; -.
DR EnsemblBacteria; BAC49954; BAC49954; BAC49954.
DR GeneID; 64024447; -.
DR KEGG; bja:bll4689; -.
DR PATRIC; fig|224911.44.peg.4516; -.
DR eggNOG; COG0809; Bacteria.
DR HOGENOM; CLU_039110_1_1_5; -.
DR InParanoid; Q89L59; -.
DR OMA; YSYGDGM; -.
DR PhylomeDB; Q89L59; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051075; F:S-adenosylmethionine:tRNA ribosyltransferase-isomerase activity; IBA:GO_Central.
DR GO; GO:0008616; P:queuosine biosynthetic process; IBA:GO_Central.
DR GO; GO:0002099; P:tRNA wobble guanine modification; IBA:GO_Central.
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..366
FT /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT isomerase"
FT /id="PRO_0000165385"
SQ SEQUENCE 366 AA; 39826 MW; FE39F4DCDEE4BDD0 CRC64;
MRTDLFDFDL PAERIALRPA SPRDSAKMLV VEGGALRDRT ISELPQWLKR GDQLVVNDTK
VIAAQLKGRR IGRETEPKIE ATLIKRLDGS RWQALVKPAK KLIAGDRIRF GNEGKVCLLG
HLDAEVEAKG SEGEVTLSFS FHGPALDQAI ADLGSPPLPP YIASKRTPDD QDFADYQTMF
AANEGAVAAP TAGLHFTPAL EQALRERGVG LNRVTLHVGA GTFLPVKVED TAGHKMHAEW
GTISAETAER LNIARHNGGR IIAVGTTSLR LLESAASEDG TIQPFAAETS IFITPGYRFR
AVDILLTNFH LPKSTLFMLV SAFSGLETMR RAYAHAIAQG YRFYSYGDAC LLFRAGGTEV
HDPSPP