QUEA_HAEDU
ID QUEA_HAEDU Reviewed; 361 AA.
AC Q7VLY1;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=HD_1257;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) 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: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; AE017143; AAP96089.1; -; Genomic_DNA.
DR RefSeq; WP_010945138.1; NC_002940.2.
DR AlphaFoldDB; Q7VLY1; -.
DR SMR; Q7VLY1; -.
DR STRING; 233412.HD_1257; -.
DR EnsemblBacteria; AAP96089; AAP96089; HD_1257.
DR KEGG; hdu:HD_1257; -.
DR eggNOG; COG0809; Bacteria.
DR HOGENOM; CLU_039110_1_0_6; -.
DR OMA; YSYGDGM; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000001022; 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..361
FT /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT isomerase"
FT /id="PRO_0000165406"
SQ SEQUENCE 361 AA; 40161 MW; 41B32F15AAEAE3E3 CRC64;
MLVSDFHFNL PDELIARYPK DERTASRLLH LNGESGKFSD LHFSDLLDHI NPGDLLIFNN
TRVIPARLYG RKESGGKLEV LIERVLDEHH CLAHIRCSKA PKAGTKLILG EDKLGIGNGL
EATMISRHDT LFELRFNATT PLFTLLQQAG HIPLPPYIDR PDEDFDQERY QTVYSKVLGA
VAAPTAGLHF DNPMLDKLKA KGVNMAFVTL HVGAGTFQPV RVENILEHNM HAEYAEVTQA
VVDQILATKA AGKRVIAVGT TSVRSIESAA QATQPTGKLI APFFSDTNIF LYPGKTFKIV
DVLITNFHLP ESTLIMLVSA FAGYRHTMNA YQHAVQQKYR FFSYGDAMLI NKNPNALNDL
P