ID K7Y427_HELPX Unreviewed; 368 AA.
AC K7Y427;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=HPAKL117_00485 {ECO:0000313|EMBL:AFX90514.1};
OS Helicobacter pylori Aklavik117.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1055531 {ECO:0000313|EMBL:AFX90514.1, ECO:0000313|Proteomes:UP000010079};
RN [1] {ECO:0000313|EMBL:AFX90514.1, ECO:0000313|Proteomes:UP000010079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aklavik117 {ECO:0000313|EMBL:AFX90514.1};
RX PubMed=25883278;
RA Kersulyte D., Bertoli M.T., Tamma S., Keelan M., Munday R., Geary J.,
RA Veldhuyzen van Zanten S., Goodman K.J., Berg D.E.;
RT "Complete Genome Sequences of Two Helicobacter pylori Strains from a
RT Canadian Arctic Aboriginal Community.";
RL Genome Announc. 3:0-0(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}.
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DR EMBL; CP003483; AFX90514.1; -; Genomic_DNA.
DR RefSeq; WP_015085352.1; NC_019560.1.
DR AlphaFoldDB; K7Y427; -.
DR KEGG; hpya:HPAKL117_00485; -.
DR PATRIC; fig|1055531.3.peg.102; -.
DR HOGENOM; CLU_056003_0_0_7; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000010079; 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 6
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT BINDING 7
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT BINDING 87
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 DISULFID 174..176
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
SQ SEQUENCE 368 AA; 42724 MW; AD07CB8A4CEBBC78 CRC64;
MLIHICCSVD NLYFLKKAKE AFAGEKMIGF FYNPNIHPYS EYLLRLEDVK RTCEMLEIEL
LEGDYELEKF LDKAKGKELL GEKSERCFEC FDLRLEASAL KAFELGEEKF TTTLLTSPKK
DPNQLIAKGQ HIAQRHNLEF VVFRNDNFEH FKSELDLNLQ ALARENELYR QNYCGCQFAL
KIQKESQNRS PFELYSPLKR QILPASVEER TQVFRALDAA KKGANKPSLA QKTIATYRLL
NGGVWLSKNS NPLNCYILAR SKSKAKVRIN DLRWVFSQRL NALVGYSQRD ETLFLTLEGL
NTLMAKNYEN LKELNLNPLN YEEELSLRAL VSGSESINPI IVLEERIERT LFVEIKSIFQ
EEKVFYLL
//
