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Database: UniProt
Entry: I3UCH6_ADVKW
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ID   I3UCH6_ADVKW            Unreviewed;       223 AA.
AC   I3UCH6;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
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   OrderedLocusNames=TKWG_12890 {ECO:0000313|EMBL:AFK62714.1};
OS   Advenella kashmirensis (strain DSM 17095 / LMG 22695 / WT001)
OS   (Tetrathiobacter kashmirensis).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae.
OX   NCBI_TaxID=1036672 {ECO:0000313|EMBL:AFK62714.1, ECO:0000313|Proteomes:UP000005267};
RN   [1] {ECO:0000313|EMBL:AFK62714.1, ECO:0000313|Proteomes:UP000005267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17095 / LMG 22695 / WT001
RC   {ECO:0000313|Proteomes:UP000005267};
RX   PubMed=21914874; DOI=10.1128/JB.05781-11;
RA   Ghosh W., George A., Agarwal A., Raj P., Alam M., Pyne P., Das Gupta S.K.;
RT   "Whole-genome shotgun sequencing of the sulfur-oxidizing chemoautotroph
RT   Tetrathiobacter kashmirensis.";
RL   J. Bacteriol. 193:5553-5554(2011).
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}.
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DR   EMBL; CP003555; AFK62714.1; -; Genomic_DNA.
DR   RefSeq; WP_014750805.1; NC_017964.1.
DR   AlphaFoldDB; I3UCH6; -.
DR   STRING; 1036672.TKWG_12890; -.
DR   KEGG; aka:TKWG_12890; -.
DR   HOGENOM; CLU_088177_0_0_4; -.
DR   OrthoDB; 9801033at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000005267; Chromosome.
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   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         26
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT   BINDING         27
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT   BINDING         105
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT   BINDING         108
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT   DISULFID        188..190
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
SQ   SEQUENCE   223 AA;  25963 MW;  93355D132C3A56EC CRC64;
     MVTVTDIERP TLALPEGHGK VLLHSCCAPC SGEVMEAMLA SGINYSIFFY NPNIHPVREY
     EIRKEENIRF AQLHGIEFID ADYDVDNWFD RVKGMENEPE RGIRCTACFD MRFERTALYA
     HEHGFDTITS SLGISRWKDM KQINGCGERA AARYPELVYW TYNWRKGGGS ARMIEISKRE
     EFYQQEYCGC VYSLRDTNRH RRAQGRDRIT IGVKFYGKQE ETL
//
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