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Database: UniProt
Entry: A0A0M4TDT2_9GAMM
LinkDB: A0A0M4TDT2_9GAMM
Original site: A0A0M4TDT2_9GAMM 
ID   A0A0M4TDT2_9GAMM        Unreviewed;       383 AA.
AC   A0A0M4TDT2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=AOC03_02575 {ECO:0000313|EMBL:ALF59066.1};
OS   Psychrobacter urativorans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=45610 {ECO:0000313|EMBL:ALF59066.1, ECO:0000313|Proteomes:UP000059847};
RN   [1] {ECO:0000313|EMBL:ALF59066.1, ECO:0000313|Proteomes:UP000059847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R10.10B {ECO:0000313|EMBL:ALF59066.1,
RC   ECO:0000313|Proteomes:UP000059847};
RA   See-Too W.S., Chan K.G.;
RT   "Complete genome of Psychrobacter urativorans R10.10B.";
RL   Submitted (SEP-2015) 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; CP012678; ALF59066.1; -; Genomic_DNA.
DR   RefSeq; WP_062533462.1; NZ_CP012678.1.
DR   AlphaFoldDB; A0A0M4TDT2; -.
DR   STRING; 45610.AOC03_02575; -.
DR   KEGG; pur:AOC03_02575; -.
DR   OrthoDB; 9805933at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000059847; 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:ALF59066.1};
KW   Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW   Rule:MF_00113};
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   383 AA;  42154 MW;  EDD5611948A30F6B CRC64;
     MTHSQHSIAN NNTDINNDGL DYLSVADYDY ELPDSLIARY PLAERSASKL LYVPASAQPE
     DHIFTALPDL LNAGDLIVFN DTKVMKARLF GKKDTGGRVE VLIERLIDNN DGTNNESETT
     QKNVALCHVK ASKAPKLGQR LILADGNMGC VMIGRQDNLF ILDFDAPILP HLEAYGELPI
     PPYFERHADA TDNIRYQTVF HDPAKLASVA APTASLHFDD GILERLAAKG INTAFVTLHV
     GAGTFAPVKT ENLLNHTMHS EYAHLPQTTA DMINQTHANG GKVIAIGTTV TRVLETAYQK
     TALNGQPLST WSGDTDIFIY PGFKFGVIDR LLTNFHLPKS TLLMLVSAFS GKSAIEQAYQ
     HAINSEYRFF SYGDAMLLDK VDF
//
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