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Database: UniProt
Entry: E2Z9B5_9FIRM
LinkDB: E2Z9B5_9FIRM
Original site: E2Z9B5_9FIRM 
ID   E2Z9B5_9FIRM            Unreviewed;       341 AA.
AC   E2Z9B5;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
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:EFQ05094.1};
GN   ORFNames=HMPREF9429_00013 {ECO:0000313|EMBL:EFQ05094.1};
OS   Megasphaera micronuciformis F0359.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=706434 {ECO:0000313|EMBL:EFQ05094.1, ECO:0000313|Proteomes:UP000003195};
RN   [1] {ECO:0000313|EMBL:EFQ05094.1, ECO:0000313|Proteomes:UP000003195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0359 {ECO:0000313|EMBL:EFQ05094.1,
RC   ECO:0000313|Proteomes:UP000003195};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2010) 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:EFQ05094.1}.
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DR   EMBL; AECS01000001; EFQ05094.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2Z9B5; -.
DR   STRING; 706434.HMPREF9429_00013; -.
DR   eggNOG; COG0809; Bacteria.
DR   HOGENOM; CLU_039110_1_0_9; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000003195; 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:EFQ05094.1};
KW   Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW   Rule:MF_00113}; Reference proteome {ECO:0000313|Proteomes:UP000003195};
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   341 AA;  38285 MW;  2F353D3CFE8E2D2C CRC64;
     MILKLSDFSY ELPQELIAQH PAEPRDTARL MLYDKKTGET ENKIFRQLTD ELHQGDVLVF
     NDSKVIPARL HGTRVPTGGK VEVLLLTPVG EDRWEVLVKP GKKALPGSTL SFGERLTGVV
     EDRTDYGGRV IHFTYDGVFD HIIEEIGEMP LPPYIHKKPE NPDDYQTVYA REKGSAAAPT
     AGLHFTDELL EKIRDKGVET VFVTLHVGLG TFRPVEEENI EDHVMHSEYY SITPEAAAAV
     NRAKEEGRRI VAVGTTSVRT LESAAEKGRL KAGAGKTNIF IYPGYTFRIV DALVTNFHLP
     ESTLLMLISA LSDREHILKA YETAVREKYR FFSFGDAMFI H
//
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