ID A0A0A7LPV1_9BACT Unreviewed; 408 AA.
AC A0A0A7LPV1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=S-adenosylmethionine:tRNA ribosyltransferase-isomerase {ECO:0000256|HAMAP-Rule:MF_00113};
DE EC=2.4.99.17 {ECO:0000256|HAMAP-Rule:MF_00113};
DE AltName: Full=Queuosine biosynthesis protein QueA {ECO:0000256|HAMAP-Rule:MF_00113};
GN Name=queA {ECO:0000256|HAMAP-Rule:MF_00113};
GN ORFNames=PK28_13920 {ECO:0000313|EMBL:AIZ64493.1};
OS Hymenobacter sp. DG25B.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1385664 {ECO:0000313|EMBL:AIZ64493.1, ECO:0000313|Proteomes:UP000030789};
RN [1] {ECO:0000313|EMBL:AIZ64493.1, ECO:0000313|Proteomes:UP000030789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG25B {ECO:0000313|EMBL:AIZ64493.1,
RC ECO:0000313|Proteomes:UP000030789};
RA Jung H.-Y., Kim M.K., Srinivasan S., Lim S.;
RT "Hymenobacter radioresistens genome sequence.";
RL Submitted (NOV-2014) 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:0000256|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 + 2 H(+) + L-
CC methionine; Xref=Rhea:RHEA:32155, Rhea:RHEA-COMP:10342, Rhea:RHEA-
CC COMP:18582, ChEBI:CHEBI:15378, ChEBI:CHEBI:16708, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:82833, ChEBI:CHEBI:194443;
CC EC=2.4.99.17; Evidence={ECO:0000256|HAMAP-Rule:MF_00113};
CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00113}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00113}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00113}.
CC -!- SIMILARITY: Belongs to the QueA family. {ECO:0000256|HAMAP-
CC Rule:MF_00113}.
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DR EMBL; CP010054; AIZ64493.1; -; Genomic_DNA.
DR RefSeq; WP_044514813.1; NZ_CP010054.1.
DR AlphaFoldDB; A0A0A7LPV1; -.
DR STRING; 1385664.PK28_13920; -.
DR KEGG; hyd:PK28_13920; -.
DR HOGENOM; CLU_039110_1_0_10; -.
DR OrthoDB; 9805933at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000030789; 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; QueA-like; 1.
DR Gene3D; 3.40.1780.10; QueA-like; 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; S-ADENOSYLMETHIONINE:TRNA RIBOSYLTRANSFERASE-ISOMERASE; 1.
DR PANTHER; PTHR30307:SF0; S-ADENOSYLMETHIONINE:TRNA RIBOSYLTRANSFERASE-ISOMERASE; 1.
DR Pfam; PF02547; Queuosine_synth; 1.
DR SUPFAM; SSF111337; QueA-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00113};
KW Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW Rule:MF_00113}; Reference proteome {ECO:0000313|Proteomes:UP000030789};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00113};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00113}.
SQ SEQUENCE 408 AA; 45216 MW; 64F3E906944CF384 CRC64;
MNANPRLLSI HDFTYQLPPE RIAPEPLPQR DQSRLLVYRE GELTDRRFYE LPTEVPTGSL
LVFNDTKVVR ARLFAHKPTG GIIELFCLEP VAPHRAIEPA MQQTGSCVWK CLVGNGKRWK
SGPVLLEFMA QGQPATLTAE RQEVADGYSL IRFSWEPAEL PFAEVLRGAG HLPLPPYLNR
PDTDVDAVRY QTVYAAQEGA VAAPTAGLHF SETVLQELQA RGIETAHVTL HVGAGTFQPV
KADRMAEHPM HAEPISVTPA FLRQLLMHSK GPVLAVGTTS LRTLESLYWL GVQLLQDPSS
ADAPLHVSQW QPYEPGSEIP AAEALQALLH YLKKTGADVL HATTQLLIAP GYRFRLAQGL
ITNFHQPEST LLLLVAALVG PQWRQLYEHA LSNDYRFLSY GDSSLLLP
//