QUEA_MACCJ
ID QUEA_MACCJ Reviewed; 340 AA.
AC B9E717;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=MCCL_1278;
OS Macrococcus caseolyticus (strain JCSC5402).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX NCBI_TaxID=458233;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC5402;
RX PubMed=19074389; DOI=10.1128/jb.01058-08;
RA Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL J. Bacteriol. 191:1180-1190(2009).
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; AP009484; BAH17985.1; -; Genomic_DNA.
DR RefSeq; WP_012657183.1; NC_011999.1.
DR AlphaFoldDB; B9E717; -.
DR SMR; B9E717; -.
DR STRING; 458233.MCCL_1278; -.
DR EnsemblBacteria; BAH17985; BAH17985; MCCL_1278.
DR KEGG; mcl:MCCL_1278; -.
DR eggNOG; COG0809; Bacteria.
DR HOGENOM; CLU_039110_1_0_9; -.
DR OMA; YSYGDGM; -.
DR OrthoDB; 368001at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000001383; 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..340
FT /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT isomerase"
FT /id="PRO_1000119158"
SQ SEQUENCE 340 AA; 38122 MW; E1B0094ADB5449FE CRC64;
MDVNEFDFNL PESLIAQTPL QDRTASRLLT LNKHTGEIKH TNFKSIIDYL NTGDTLVLND
TKVMPARLFG VKEDTGAKIE MLMLTEHDNG WEVLIKPAKR VTIGTRISFG EGKIVAICVE
ELDQGGRIMQ LNYEGILQER LDELGLMPLP PYIKETLEDQ SRYQTVYARA TGSAAAPTAG
LHFTESLLED IKAKGINIAY ITLHVGLGTF RPVSVDDVES HKMHSEYYEM SEETAKLLND
TRDSGNRIIT VGTTSTRTLE TIADDSGHFT AQSGWTDIFI YPGYSFKAVD AMITNFHLPK
STLVMLVSSL ATKEFIMNAY NEAVNEKYRF FSFGDAMFIY