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Entry: A0A0B2BZ04_9SPHN
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ID   A0A0B2BZ04_9SPHN        Unreviewed;       227 AA.
AC   A0A0B2BZ04;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=PK98_02625 {ECO:0000313|EMBL:KHL26679.1};
OS   Croceibacterium mercuriale.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Croceibacterium.
OX   NCBI_TaxID=1572751 {ECO:0000313|EMBL:KHL26679.1, ECO:0000313|Proteomes:UP000030988};
RN   [1] {ECO:0000313|EMBL:KHL26679.1, ECO:0000313|Proteomes:UP000030988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Coronado {ECO:0000313|EMBL:KHL26679.1,
RC   ECO:0000313|Proteomes:UP000030988};
RA   Coil D.A., Eisen J.A.;
RT   "Draft genome sequence of Kirrobacter mercurialis.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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:KHL26679.1}.
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DR   EMBL; JTDN01000001; KHL26679.1; -; Genomic_DNA.
DR   RefSeq; WP_039096147.1; NZ_JTDN01000001.1.
DR   AlphaFoldDB; A0A0B2BZ04; -.
DR   STRING; 1572751.PK98_02625; -.
DR   OrthoDB; 9801033at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000030988; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000030988};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_02089}.
FT   BINDING         29
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT   BINDING         30
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   BINDING         111
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT   DISULFID        191..193
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
SQ   SEQUENCE   227 AA;  25950 MW;  D6E87827BFFF13BF CRC64;
     MTDQPVTTPI DRPVLIPPEA QGRVLLHSCC APCSGEVMEA MTASGIDYAI FFYNPNIHPK
     EEYILRKEEN IRFAEKHGIP FIDADYDTAN WFKRARGMEM EPERGARCTM CFDMRFERTA
     LYAHENGFPV ITSSLGISRW KNMTQINGCG ERAAAHYPGI TYWTFNWRKG GGAARMIEIS
     KREQFYQQEY CGCVYSLRDT NAHRVSQGRE EIRMGEMFYG VEGPGEG
//
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