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Database: UniProt
Entry: V7ZM45_ENTFL
LinkDB: V7ZM45_ENTFL
Original site: V7ZM45_ENTFL 
ID   V7ZM45_ENTFL            Unreviewed;       395 AA.
AC   V7ZM45;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Epoxyqueuosine reductase {ECO:0000256|HAMAP-Rule:MF_00916};
DE            EC=1.17.99.6 {ECO:0000256|HAMAP-Rule:MF_00916};
DE   AltName: Full=Queuosine biosynthesis protein QueG {ECO:0000256|HAMAP-Rule:MF_00916};
GN   Name=queG {ECO:0000256|HAMAP-Rule:MF_00916};
GN   ORFNames=T481_10385 {ECO:0000313|EMBL:ETC91813.1};
OS   Enterococcus faecalis PF3.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1410655 {ECO:0000313|EMBL:ETC91813.1, ECO:0000313|Proteomes:UP000018533};
RN   [1] {ECO:0000313|EMBL:ETC91813.1, ECO:0000313|Proteomes:UP000018533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF3 {ECO:0000313|EMBL:ETC91813.1,
RC   ECO:0000313|Proteomes:UP000018533};
RX   PubMed=24459271;
RA   Spence R.J., Pavasovic A., Smith J.J., Prentis P.J.;
RT   "Draft Genome Sequence of Enterococcus faecalis Strain PF3, Isolated from
RT   Adelie Penguin Feces from Antarctica.";
RL   Genome Announc. 2:e01209-13(2014).
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). {ECO:0000256|HAMAP-
CC       Rule:MF_00916}.
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|HAMAP-Rule:MF_00916};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00916};
CC       Note=Binds 2 [4Fe-4S] clusters per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_00916};
CC   -!- COFACTOR:
CC       Name=cob(II)alamin; Xref=ChEBI:CHEBI:16304;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00916};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00916}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00916}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00916}.
CC   -!- SIMILARITY: Belongs to the QueG family. {ECO:0000256|HAMAP-
CC       Rule:MF_00916}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00916}.
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:ETC91813.1}.
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DR   EMBL; AZIA01000212; ETC91813.1; -; Genomic_DNA.
DR   AlphaFoldDB; V7ZM45; -.
DR   PATRIC; fig|1410655.3.peg.1956; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000018533; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
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   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   HAMAP; MF_00916; QueG; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR004155; PBS_lyase_HEAT.
DR   InterPro; IPR004453; QueG.
DR   InterPro; IPR013542; QueG_DUF1730.
DR   NCBIfam; TIGR00276; tRNA epoxyqueuosine(34) reductase QueG; 1.
DR   PANTHER; PTHR30002; EPOXYQUEUOSINE REDUCTASE; 1.
DR   PANTHER; PTHR30002:SF4; EPOXYQUEUOSINE REDUCTASE; 1.
DR   Pfam; PF13484; Fer4_16; 1.
DR   Pfam; PF13646; HEAT_2; 1.
DR   Pfam; PF08331; QueG_DUF1730; 1.
DR   SMART; SM00567; EZ_HEAT; 2.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Cobalamin {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Cobalt {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00916};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00916};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_00916};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00916}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785, ECO:0000256|HAMAP-
KW   Rule:MF_00916};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00916}.
FT   DOMAIN          187..216
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   ACT_SITE        142
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         61
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         142
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         163
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         166
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         177
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         196
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         199
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         202
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         206
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         222
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         224
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         228
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         230
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         248..249
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         248
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         251
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         255
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         288
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         289
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         303
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         305
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         306
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
SQ   SEQUENCE   395 AA;  44654 MW;  99FAFF8FC57D92C4 CRC64;
     MKGGMSNATL KEKIIQESQR LGIDKIGFTH AEPFIELEDS LHEQRERGYN SGFEHQNVEE
     RIYPEKTFEH PKSIISIALA YPTKAQGKMP RDEKRGQFAR ASWGIDYHHI LQDRLQKLIA
     FIEEQAATEA EKEHWRFRPQ VDTGEYVDTA VAQRAGLGFI GKNGLLITEE FGSFVYLGEV
     TTNIQFEPDE PVPNGCGDCT RCITGCPTGA LLGDGRMNAQ KCLSYQTQTK GMMPEEYRKK
     MRNVIYGCDI CQLVCPYNKG KDFHFHEEME PKIEEVYPKL APLLTISNKE FKQQFGHLAG
     SWRGKKPLQR NALIALANLG GREAIPQIIL CLNDQRPVIR GTAAWSLGQL AKREPEQSLE
     ALNYLLSVET EAEVIEEAQK AIYLLTSKKG SRSTE
//
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