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Database: UniProt
Entry: A0A1Y4HNU4_9ACTN
LinkDB: A0A1Y4HNU4_9ACTN
Original site: A0A1Y4HNU4_9ACTN 
ID   A0A1Y4HNU4_9ACTN        Unreviewed;       408 AA.
AC   A0A1Y4HNU4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   13-SEP-2023, entry version 24.
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=B5F33_05150 {ECO:0000313|EMBL:OUP09126.1};
OS   Collinsella sp. An2.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC   Coriobacteriaceae; Collinsella.
OX   NCBI_TaxID=1965585 {ECO:0000313|EMBL:OUP09126.1, ECO:0000313|Proteomes:UP000195399};
RN   [1] {ECO:0000313|Proteomes:UP000195399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An2 {ECO:0000313|Proteomes:UP000195399};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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}.
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:OUP09126.1}.
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DR   EMBL; NFJW01000006; OUP09126.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4HNU4; -.
DR   OrthoDB; 9783887at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000195399; 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:OUP09126.1};
KW   Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW   Rule:MF_00113}; Reference proteome {ECO:0000313|Proteomes:UP000195399};
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   408 AA;  44597 MW;  A747F26B2F5D9F86 CRC64;
     MRTDDFDYDL PDELIAQAPA DPRDSCRLLV LHRDDEPLAT ASQTVPLRHG GSVEHRHFYD
     IADYLEPGDL LVANKTRVMP ARLVGHKAGT GGVAETLLLK RREDVDALGH VWECLVNPGR
     RLKPGAVIEY RAGGLHAPAS SPVVLTGTVV DFVPESRGGR LVRFEPVGEG VDGRPRTLDE
     AIHAAGHVPL PPYITQYEGD PEKYQTVYAM QEEHSAAAPT AGLHFTPELI ASLEDKGIGF
     VTVELEVGID TFRLVEEDDP TQHVMHTERY HVPADVVEAV HATKAAGHRV IAVGTTAVRS
     LESAWDPDAP ASDPAVVARR FEQAPDSAAV TGRGDIVPRE NATTNLYLMP GSTYHVVDAL
     ITNFHVPRST LMMLVSALAT RDQIMDAYEQ AIAERYRFLS FGDAMFIE
//
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