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Database: UniProt
Entry: S5R6X4_9STRE
LinkDB: S5R6X4_9STRE
Original site: S5R6X4_9STRE 
ID   S5R6X4_9STRE            Unreviewed;       276 AA.
AC   S5R6X4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=KE3_1894 {ECO:0000313|EMBL:AGS06345.1};
OS   Streptococcus lutetiensis 033.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1076934 {ECO:0000313|EMBL:AGS06345.1, ECO:0000313|Proteomes:UP000015268};
RN   [1] {ECO:0000313|EMBL:AGS06345.1, ECO:0000313|Proteomes:UP000015268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=033 {ECO:0000313|EMBL:AGS06345.1,
RC   ECO:0000313|Proteomes:UP000015268};
RX   PubMed=23782707; DOI=10.1186/1471-2180-13-141;
RA   Jin D., Chen C., Li L., Lu S., Li Z., Zhou Z., Jing H., Xu Y., Du P.,
RA   Wang H., Xiong Y., Zheng H., Bai X., Sun H., Wang L., Ye C., Gottschalk M.,
RA   Xu J.;
RT   "Dynamics of fecal microbial communities in children with diarrhea of
RT   unknown etiology and genomic analysis of associated Streptococcus
RT   lutetiensis.";
RL   BMC Microbiol. 13:141-141(2013).
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; CP003025; AGS06345.1; -; Genomic_DNA.
DR   AlphaFoldDB; S5R6X4; -.
DR   KEGG; slu:KE3_1894; -.
DR   PATRIC; fig|1076934.5.peg.1863; -.
DR   HOGENOM; CLU_088177_1_0_9; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000015268; 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         65
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT   BINDING         66
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT   BINDING         149
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT   BINDING         152
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT   DISULFID        231..233
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
SQ   SEQUENCE   276 AA;  32237 MW;  D4B4F72EB7F14875 CRC64;
     MKNNLWYNGV TSSVLERKTI FVIDLEEILS RMNPNQKINY DRVMQQMAKR WAQEEVRPKI
     LVHVCCAPCS TYTLEYLTQY ADVTVYFANS NIHPRDEYLR RAYVVQKFIS EFNEKTENTV
     DFIEAPYDPS EYFQKVHGLE EEPEGGERCT ACFDYRLDKA AQKAVELGYD YFASALTISP
     HKNSQVINSV GVEVQKVYAT KYLPSDFKKN NGYRRSVEMC EEYDIYRQCY CGCVFAAKMQ
     GVDLNQIKKE AKEFMVGKDG EKEFPHIRFT FEGKEI
//
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