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Database: UniProt
Entry: A0A0G0T1X9_9BACT
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ID   A0A0G0T1X9_9BACT        Unreviewed;       301 AA.
AC   A0A0G0T1X9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=UT64_C0049G0011 {ECO:0000313|EMBL:KKR31837.1};
OS   Candidatus Falkowbacteria bacterium GW2011_GWF2_39_8.
OC   Bacteria; Candidatus Falkowbacteria.
OX   NCBI_TaxID=1618642 {ECO:0000313|EMBL:KKR31837.1, ECO:0000313|Proteomes:UP000034137};
RN   [1] {ECO:0000313|EMBL:KKR31837.1, ECO:0000313|Proteomes:UP000034137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(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}.
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:KKR31837.1}.
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DR   EMBL; LBXO01000049; KKR31837.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0T1X9; -.
DR   PATRIC; fig|1618642.3.peg.833; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000034137; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   NCBIfam; NF037970; vanZ_1; 1.
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   Membrane {ECO:0000256|SAM:Phobius};
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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_02089}.
FT   TRANSMEM        40..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        100..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         132
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT   BINDING         133
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT   BINDING         210
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT   BINDING         213
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
FT   DISULFID        292..294
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02089"
SQ   SEQUENCE   301 AA;  35207 MW;  BBE91D2A9A634EB4 CRC64;
     MIKFAKVFLL VCWLSLILKL LTFPNPETNP FFQFPLSDKF IHLVLFGGLV YFMLEVIEAF
     FVLRYSFVVF WGLVFSIGYA FLLEYLQNFI PGRSSSSSDI LAAILGSVLA IVVIYFLDYK
     NLKKPKLLIQ ICCIGCGAYV VKLLKEQYRL ALYFYNPNIY PKSEYNRRLK ETRRIAHKLG
     LKLIIGKYRY PFWLEKIKGH ESDPERGGRC IICYRERLEE TARLAKRLKY DYFGSTLTIS
     PHKSAPAINQ LGKELAESYQ VQYLESDFKK CDGFKKSVEL SQELKLYRQN YCGCEFSMKR
     E
//
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