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Database: UniProt
Entry: F5LAQ4_CALTT
LinkDB: F5LAQ4_CALTT
Original site: F5LAQ4_CALTT 
ID   F5LAQ4_CALTT            Unreviewed;       342 AA.
AC   F5LAQ4;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
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=CathTA2_2989 {ECO:0000313|EMBL:EGL81626.1};
OS   Caldalkalibacillus thermarum (strain TA2.A1).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldalkalibacillus.
OX   NCBI_TaxID=986075 {ECO:0000313|EMBL:EGL81626.1, ECO:0000313|Proteomes:UP000010716};
RN   [1] {ECO:0000313|EMBL:EGL81626.1, ECO:0000313|Proteomes:UP000010716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TA2.A1 {ECO:0000313|EMBL:EGL81626.1,
RC   ECO:0000313|Proteomes:UP000010716};
RX   PubMed=21685297; DOI=10.1128/JB.05035-11;
RA   Kalamorz F., Keis S., McMillan D.G., Olsson K., Stanton J.A., Stockwell P.,
RA   Black M.A., Klingeman D.M., Land M.L., Han C.S., Martin S.L., Becher S.A.,
RA   Peddie C.J., Morgan H.W., Matthies D., Preiss L., Meier T., Brown S.D.,
RA   Cook G.M.;
RT   "Draft genome sequence of the thermoalkaliphilic Caldalkalibacillus
RT   thermarum strain TA2.A1.";
RL   J. Bacteriol. 193:4290-4291(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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGL81626.1}.
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DR   EMBL; AFCE01000164; EGL81626.1; -; Genomic_DNA.
DR   RefSeq; WP_007506355.1; NZ_AFCE01000164.1.
DR   AlphaFoldDB; F5LAQ4; -.
DR   eggNOG; COG0809; Bacteria.
DR   OrthoDB; 9805933at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000010716; Unassembled WGS sequence.
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:EGL81626.1};
KW   Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW   Rule:MF_00113}; Reference proteome {ECO:0000313|Proteomes:UP000010716};
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   342 AA;  38379 MW;  4239FFD56E33FACB CRC64;
     MRVDEFDFEL PEELIAQKPL PDRASSRLLH LDRQTGAIFH HQFTDIVQLL TAGDVLVLND
     TKVMPARLLG VKEETGAKVE VLLLKQIEGD SWETLVKPAK RVKPGVTLRF GDGRLRAVCT
     GVTDAGGRYI RFEYQGIFQE ILAELGQMPL PPYIKEQLDD PDRYQTVYAR HEGSAAAPTA
     GLHFTPAILQ ALEDKGVILT YITLHVGLGT FRPVQAERVE EHQMHAEFFQ MPQETAQVLN
     QAKAEGRRII AVGTTSVRTL ETVVRAQNGR FGACSGWTDI FIYPGFRFQA IDGMLTNFHL
     PKSTLIMLVS AFAGKETIMQ AYREAVKQRY RFFSFGDAML IL
//
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