ID D7DLW2_METV0 Unreviewed; 350 AA.
AC D7DLW2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 70.
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 OrderedLocusNames=M301_2291 {ECO:0000313|EMBL:ADI30656.1};
OS Methylotenera versatilis (strain 301).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylotenera.
OX NCBI_TaxID=666681 {ECO:0000313|EMBL:ADI30656.1, ECO:0000313|Proteomes:UP000000383};
RN [1] {ECO:0000313|Proteomes:UP000000383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 {ECO:0000313|Proteomes:UP000000383};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Clum A., Land M., Hauser L., Kyrpides N., Ivanova N.,
RA Chistoservova L., Kalyuzhnaya M., Woyke T.;
RT "Complete sequence of Methylotenera sp. 301.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADI30656.1, ECO:0000313|Proteomes:UP000000383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 {ECO:0000313|EMBL:ADI30656.1,
RC ECO:0000313|Proteomes:UP000000383};
RX PubMed=21622745; DOI=10.1128/JB.00404-11;
RA Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT "Genomes of three methylotrophs from a single niche uncover genetic and
RT metabolic divergence of Methylophilaceae.";
RL J. Bacteriol. 193:3757-3764(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002056; ADI30656.1; -; Genomic_DNA.
DR RefSeq; WP_013148964.1; NC_014207.1.
DR AlphaFoldDB; D7DLW2; -.
DR STRING; 666681.M301_2291; -.
DR KEGG; meh:M301_2291; -.
DR eggNOG; COG0809; Bacteria.
DR HOGENOM; CLU_039110_1_0_4; -.
DR OrthoDB; 9805933at2; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000000383; 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 Isomerase {ECO:0000313|EMBL:ADI30656.1};
KW Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW Rule:MF_00113}; Reference proteome {ECO:0000313|Proteomes:UP000000383};
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 350 AA; 38770 MW; 0772820F313DDC0C CRC64;
MRTEDFNFYL PDALIAQHPT AERTASRMLH LNSSKGELAD NMFINLPEHL QAGDLLVFND
TRVIKARLFG VKHTGGSVEV MIERVINQHT AYAQIRASRA PKVGTRLTLS NAFDVEVTAR
HDDLFELLFL SETSVLDLLE QHGALPLPPY ITHSATSDDE ERYQTVFSKH LGAVAAPTAG
LHFNDAMLDT LKQKGINIAY VTLHVGAGTF QPVRVDNINE HKMHSELYSI SQATIDMINA
TKTNGAKVTA IGTTALRALE SAARVTEFNT NGNLQAGNGD TDIFITPGYQ FKVVDRLFTN
FHLPKSTLLM LVSAFAGMDN IKKAYEHAIN EHYRFFSYGD AMLIEKHPAA
//