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Database: UniProt
Entry: A0A223VBW2_9FLAO
LinkDB: A0A223VBW2_9FLAO
Original site: A0A223VBW2_9FLAO 
ID   A0A223VBW2_9FLAO        Unreviewed;       350 AA.
AC   A0A223VBW2;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
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   ECO:0000313|EMBL:GGD95339.1};
GN   ORFNames=CJ263_13395 {ECO:0000313|EMBL:ASV32700.1}, GCM10011412_36790
GN   {ECO:0000313|EMBL:GGD95339.1};
OS   Maribacter cobaltidurans.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=1178778 {ECO:0000313|EMBL:ASV32700.1, ECO:0000313|Proteomes:UP000215244};
RN   [1] {ECO:0000313|EMBL:ASV32700.1, ECO:0000313|Proteomes:UP000215244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B1 {ECO:0000313|EMBL:ASV32700.1,
RC   ECO:0000313|Proteomes:UP000215244};
RA   Wu Y.-H., Cheng H., Xu X.-W.;
RT   "The complete genome sequence of Maribacter sp. B1, isolated from deep-sea
RT   sediment.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GGD95339.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.15508 {ECO:0000313|EMBL:GGD95339.1};
RX   PubMed=30832757;
RA   Wu L., Ma J.;
RT   "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT   project: providing services to taxonomists for standard genome sequencing
RT   and annotation.";
RL   Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN   [3] {ECO:0000313|EMBL:GGD95339.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.15508 {ECO:0000313|EMBL:GGD95339.1};
RA   Sun Q., Zhou Y.;
RL   Submitted (DEC-2022) 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; CP022957; ASV32700.1; -; Genomic_DNA.
DR   EMBL; BMJL01000012; GGD95339.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A223VBW2; -.
DR   KEGG; marb:CJ263_13395; -.
DR   OrthoDB; 9805933at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000215244; Chromosome.
DR   Proteomes; UP000603042; 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:ASV32700.1};
KW   Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW   Rule:MF_00113}; Reference proteome {ECO:0000313|Proteomes:UP000215244};
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;  40381 MW;  7EA7431F4E3EC941 CRC64;
     MKLSNFNFEL PKELLAEHPS ENRDESKLMV IDTKTGKIEH KMFKDMIDYF DEGDVMVLNN
     TKVFPARLYG NKEKTGARIE VFLLRELNEE QRLWDVLVDP ARKIRIGNKL YFGDDETLVA
     EVIDNTTSRG RTLRFLYDGA YLDFRRKLRE LGETPLPKYI KRDVEPEDEE RYQTIYAKHE
     GAVAAPTAGL HFSKHLLKRL EIKGIDFAEL TLHVGLGTFN PVEVEDLSKH KMDSEELIID
     EKATEIVNNA IEKKRRICAV GTTAMRGLES AVSSNHTLNT FEGWTNKFIF PPYEFSIANS
     MITNFHLPKS TLLMMISAFM GHDLMKKAYK EAIMEGYKFY SYGDAMLILR
//
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