ID F0KNY3_ACICP Unreviewed; 345 AA.
AC F0KNY3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 ECO:0000313|EMBL:ADY82958.1};
GN OrderedLocusNames=BDGL_002372 {ECO:0000313|EMBL:ADY82958.1};
OS Acinetobacter calcoaceticus (strain PHEA-2).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=871585 {ECO:0000313|EMBL:ADY82958.1, ECO:0000313|Proteomes:UP000007477};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PHEA-2;
RA Zhan Y., Yan Y., Zhang W., Chen M., Ping S., Lu W., Lin M.;
RT "The genome sequence of a nonpathogenic wastewater-adapted bacterium
RT Acinetobacter calcoaceticus PHEA-2 and comparative genomics insights into
RT environmental adaptation.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADY82958.1, ECO:0000313|Proteomes:UP000007477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHEA-2 {ECO:0000313|EMBL:ADY82958.1,
RC ECO:0000313|Proteomes:UP000007477};
RX PubMed=21441526; DOI=10.1128/JB.00261-11;
RA Zhan Y., Yan Y., Zhang W., Yu H., Chen M., Lu W., Ping S., Peng Z.,
RA Yuan M., Zhou Z., Elmerich C., Lin M.;
RT "Genome sequence of Acinetobacter calcoaceticus PHEA-2, isolated from
RT industry wastewater.";
RL J. Bacteriol. 193:2672-2673(2011).
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; CP002177; ADY82958.1; -; Genomic_DNA.
DR RefSeq; WP_014207644.1; NC_016603.1.
DR RefSeq; YP_004996640.1; NC_016603.1.
DR AlphaFoldDB; F0KNY3; -.
DR STRING; 871585.BDGL_002372; -.
DR GeneID; 11636904; -.
DR KEGG; acc:BDGL_002372; -.
DR PATRIC; fig|871585.3.peg.2374; -.
DR eggNOG; COG0809; Bacteria.
DR HOGENOM; CLU_039110_1_0_6; -.
DR OrthoDB; 9805933at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000007477; 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 NCBIfam; TIGR00113; queA; 1.
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:UP000007477};
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 345 AA; 38806 MW; 98D8AE32134FA9D6 CRC64;
MQLSDFSFEL PDELIARYPL ESRSASRLLH LDSKGQYHDH MFTDIIDLFE EGDLLVLNDT
KVMKARLKGK RSTGGAIEIL VERMLNHTTA YCHIKSSNSP KADAELFVGA DNIPVIVRGR
HENLFVVEFS QPILPVLEQY GQLPIPPYFN REAEEIDTER YQTVFHNPEK IASVAAPTAS
LHFDEELLAK LEQKNVQKSF VTLHVGAGTF MPVRTDDITN HVMHSEWCDV PQETIDLILA
TKARGNKVIA VGTTATRALE SAAQAHGGKI AAWTGDTQIF IYPGYEFCIV DRLITNFHLP
ESTLLMLVSA LSNRDNILAA YEHAVKSRYR FFSYGDAMLI DKLEV
//
