ID A0A101FL92_9BACT Unreviewed; 183 AA.
AC A0A101FL92;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Epoxyqueuosine reductase QueH {ECO:0000256|ARBA:ARBA00016895, ECO:0000256|HAMAP-Rule:MF_02089};
DE EC=1.17.99.6 {ECO:0000256|ARBA:ARBA00012622, ECO:0000256|HAMAP-Rule:MF_02089};
DE AltName: Full=Queuosine biosynthesis protein QueH {ECO:0000256|ARBA:ARBA00031446, ECO:0000256|HAMAP-Rule:MF_02089};
GN Name=queH {ECO:0000256|HAMAP-Rule:MF_02089};
GN ORFNames=XD68_1333 {ECO:0000313|EMBL:KUK39105.1};
OS Synergistales bacterium 54_24.
OC Bacteria; Synergistota; Synergistia; Synergistales.
OX NCBI_TaxID=1635272 {ECO:0000313|EMBL:KUK39105.1, ECO:0000313|Proteomes:UP000054050};
RN [1] {ECO:0000313|Proteomes:UP000054050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
CC -!- FUNCTION: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine
CC (Q), which is a hypermodified base found in the wobble positions of
CC tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
CC {ECO:0000256|ARBA:ARBA00002268, ECO:0000256|HAMAP-Rule:MF_02089}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in
CC tRNA; Xref=Rhea:RHEA:32159, Rhea:RHEA-COMP:18571, Rhea:RHEA-
CC COMP:18582, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:194431, ChEBI:CHEBI:194443; EC=1.17.99.6;
CC Evidence={ECO:0000256|ARBA:ARBA00035072, ECO:0000256|HAMAP-
CC Rule:MF_02089};
CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004691, ECO:0000256|HAMAP-Rule:MF_02089}.
CC -!- SIMILARITY: Belongs to the QueH family. {ECO:0000256|ARBA:ARBA00008207,
CC ECO:0000256|HAMAP-Rule:MF_02089}.
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:KUK39105.1}.
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DR EMBL; LGFQ01000072; KUK39105.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101FL92; -.
DR STRING; 1635272.XD68_1333; -.
DR PATRIC; fig|1635272.3.peg.1547; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000054050; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0052693; F:epoxyqueuosine reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR CDD; cd01986; Alpha_ANH_like; 1.
DR HAMAP; MF_02089; QueH; 1.
DR InterPro; IPR003828; QueH.
DR PANTHER; PTHR36701; EPOXYQUEUOSINE REDUCTASE QUEH; 1.
DR PANTHER; PTHR36701:SF1; EPOXYQUEUOSINE REDUCTASE QUEH; 1.
DR Pfam; PF02677; QueH; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_02089};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW Rule:MF_02089}; Iron {ECO:0000256|HAMAP-Rule:MF_02089};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02089};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02089};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_02089}; Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02089};
KW Redox-active center {ECO:0000256|HAMAP-Rule:MF_02089};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_02089}.
FT BINDING 11
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT BINDING 90
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT BINDING 93
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT DISULFID 172..174
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
SQ SEQUENCE 183 AA; 20534 MW; F8153DE87E5755AC CRC64;
MTAEKALLHI CCAPDATIPW RVLVDEGLDV VGYFYGSNIH PADEYSKRRE AVEKLAREMG
SSVIFAPYEP EAWLERTRHL AEEPEGGKRC ALCFALQLES ALAEALRRRC DAMATSLTIS
PHKDPDTINA LGRALCRAAG IEWVSRTWRK RGGFALSVEE SRRLGLYRQK YCGCIYSIPK
KEG
//