QUEA_AZOPC
ID QUEA_AZOPC Reviewed; 354 AA.
AC B6YR69;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 25-MAY-2022, entry version 64.
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=CFPG_428;
OS Azobacteroides pseudotrichonymphae genomovar. CFP2.
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC Candidatus Azobacteroides.
OX NCBI_TaxID=511995;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19008447; DOI=10.1126/science.1165578;
RA Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T.,
RA Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT "Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT
RT protist cells in termite gut.";
RL Science 322:1108-1109(2008).
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; AP010656; BAG83691.1; -; Genomic_DNA.
DR RefSeq; WP_012573452.1; NC_011565.1.
DR AlphaFoldDB; B6YR69; -.
DR SMR; B6YR69; -.
DR STRING; 511995.CFPG_428; -.
DR EnsemblBacteria; BAG83691; BAG83691; CFPG_428.
DR KEGG; aps:CFPG_428; -.
DR eggNOG; COG0809; Bacteria.
DR HOGENOM; CLU_039110_1_0_10; -.
DR OMA; LSKHKMD; -.
DR OrthoDB; 368001at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000000723; 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..354
FT /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT isomerase"
FT /id="PRO_1000117522"
SQ SEQUENCE 354 AA; 40812 MW; A10A6B1C5D2D8184 CRC64;
MRLSKFKFHL PQELIALFPS VDRDESRLMV VYHKTGRVEH VIFKDIIQYF NEKDTFIFND
TSVIPARLNG NKEKTGARVE VFLLRELDPI QRIWDVLVDP ARKIRIGNKL YFENEDSDTI
VAEIIDNTTS RGRIIRFLYD GPYESFKKIL YNLGNMPIPD YLDRKVTKED RERYQTIYAK
NEGAVVAPAA GLHFSHELMK RLELKGCELT FITVHSGMGN FRAIDVEDLF KYKSESERIV
INTETATKIN QAKQNRKQIC AVGTSVLRTI EDRENVVTSQ GYLNPFTGWT NKFIFPPYNF
ITSTSLITGF HLPLSSMLLQ VAAFGGFDLI MDVYKQAIEA KYRFGVYGDA MLII
