QUEA_PROM5
ID QUEA_PROM5 Reviewed; 373 AA.
AC A2BV65;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=P9515_04671;
OS Prochlorococcus marinus (strain MIT 9515).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167542;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9515;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000552; ABM71676.1; -; Genomic_DNA.
DR RefSeq; WP_011819784.1; NC_008817.1.
DR AlphaFoldDB; A2BV65; -.
DR SMR; A2BV65; -.
DR STRING; 167542.P9515_04671; -.
DR PRIDE; A2BV65; -.
DR EnsemblBacteria; ABM71676; ABM71676; P9515_04671.
DR KEGG; pmc:P9515_04671; -.
DR eggNOG; COG0809; Bacteria.
DR HOGENOM; CLU_039110_1_0_3; -.
DR OMA; YSYGDGM; -.
DR OrthoDB; 368001at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000001589; 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; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..373
FT /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT isomerase"
FT /id="PRO_1000094800"
SQ SEQUENCE 373 AA; 42471 MW; 79E61B56DC8731A3 CRC64;
MNFEIYNEEI DHKLEAYDYC LDESLIAGKP SKVRHESRLM IVRDSSLKED YSTNKYTKDL
LAELREGDLV VINDTKVMKA RLKVELENGQ LVELLVLEKS DQSTWLCLAK PAKKLKINKQ
LNLKSPFAKD IKLKISGIDD ETGGRFIKFP ENINDLISMN KLLDIFGEIP IPPYIKSSEE
ESFHENSYQT EYACNPGAVA APTAGLHLSK SLISNLKKKG ILVMPITLHV GYGTFKPIDQ
EDLSDLKLHK EWVSVSKKVV EEIKRIKKTD RRVIAIGTTS VRALESCYSY AMKDFIPIAK
YVDLVIKPGY KFKAVDGLLT NFHLPKSSLL LLVSAMIGRE RLLDLYKKAT KEKFRFFSYG
DAMYISPDSF LEK