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Entry: A0A2K8VEK4_9FLAO
LinkDB: A0A2K8VEK4_9FLAO
Original site: A0A2K8VEK4_9FLAO 
ID   A0A2K8VEK4_9FLAO        Unreviewed;       349 AA.
AC   A0A2K8VEK4;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=BTO06_13535 {ECO:0000313|EMBL:AUC16116.1};
OS   Tenacibaculum sp. SZ-18.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=754423 {ECO:0000313|EMBL:AUC16116.1, ECO:0000313|Proteomes:UP000232695};
RN   [1] {ECO:0000313|EMBL:AUC16116.1, ECO:0000313|Proteomes:UP000232695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZ-18 {ECO:0000313|EMBL:AUC16116.1,
RC   ECO:0000313|Proteomes:UP000232695};
RA   Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT   "Trade-off between light-utilization and light-protection in marine
RT   flavobacteria.";
RL   Submitted (DEC-2016) 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; CP019335; AUC16116.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K8VEK4; -.
DR   OrthoDB; 9805933at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000232695; 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:AUC16116.1};
KW   Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW   Rule:MF_00113}; Reference proteome {ECO:0000313|Proteomes:UP000232695};
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   349 AA;  40352 MW;  C490AB74D8778385 CRC64;
     MKLSQFNFEL PKELLAEYPS EHRDEARLMV LNRKEQTIEH KLFKDLINYF DEGDVMMLNN
     TKVFPARMFG NKEKTGARIE VFLLRELNAE HRLWDVLVDP ARKIRIGNKL FFGEDESLVA
     EVIDNTTSRG RTLRFLFDGS YEEFRKKLIE LGETPLPKYI KREVEPEDEE RYQTIYAKHE
     GAVAAPTAGL HFSKHLMKRL EIKGVDFAEM TLHVGLGTFN PVEVEDLSKH KMDSEQIIIP
     EEACNIVNNA IEKKRRVCAV GTTVMRTVES SVSASHRLNA YNGWTNKFIF PPYDFSIANC
     MVTNFHTPKS TLLMMIAAFA GYDFVMEAYE EAVKEKYKFY SYGDAMLII
//
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