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Database: UniProt
Entry: M5Z1Y8_HELPX
LinkDB: M5Z1Y8_HELPX
Original site: M5Z1Y8_HELPX 
ID   M5Z1Y8_HELPX            Unreviewed;       368 AA.
AC   M5Z1Y8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=HMPREF1436_01065 {ECO:0000313|EMBL:EMJ43425.1};
OS   Helicobacter pylori GAMchJs136i.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1159064 {ECO:0000313|EMBL:EMJ43425.1, ECO:0000313|Proteomes:UP000011924};
RN   [1] {ECO:0000313|EMBL:EMJ43425.1, ECO:0000313|Proteomes:UP000011924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAMchJs136i {ECO:0000313|EMBL:EMJ43425.1,
RC   ECO:0000313|Proteomes:UP000011924};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Antonio M., Secka O.,
RA   Thomas J., Warren W., Mitreva M., Mardis E.R., Wilson R.K.;
RL   Submitted (NOV-2012) 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:EMJ43425.1}.
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DR   EMBL; APEM01000059; EMJ43425.1; -; Genomic_DNA.
DR   RefSeq; WP_001978731.1; NZ_KB644643.1.
DR   AlphaFoldDB; M5Z1Y8; -.
DR   PATRIC; fig|1159064.3.peg.1017; -.
DR   HOGENOM; CLU_056003_0_0_7; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000011924; 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   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;  42758 MW;  4AFCEBE46FEFF973 CRC64;
     MLIHICCSVD NLYFLKKAKE AFAGEKIVGF FYNPNIHPYS EYLLRLEDVK RTCEMLEIEL
     LEGEYELEKF LDKAKGKELL GEKSERCFEC FDLRLEASAL KAFELGEERF TTTLLTSPKK
     DPNQLIAKGQ SIAQRHNLEF VVFRNDNFEH FKSELDLNLQ ALARENELYR QNYCGCQFAL
     KIQKESQNRS PFELYSPLKR QILPASIEER TQVFRTLETA KKNGNKPFLA QKTITTYRLL
     SGGVWLSKNS NPLNCYILVR SKSKAKVRIN DLRWVFSQRL SALVGYSQRD ETLFLTLEGL
     NTLMAKNYDN LKELNLNPLN YEEELSLRAL VSGSESINPI IVLEECTEKT LFVEIKSVFQ
     EEKVFYLL
//
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