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Database: UniProt
Entry: A0A1V1ZGT5_9FLAO
LinkDB: A0A1V1ZGT5_9FLAO
Original site: A0A1V1ZGT5_9FLAO 
ID   A0A1V1ZGT5_9FLAO        Unreviewed;       307 AA.
AC   A0A1V1ZGT5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=BKM32_06435 {ECO:0000313|EMBL:OMP31361.1};
OS   Mangrovimonas sp. DI 80.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Mangrovimonas.
OX   NCBI_TaxID=1779330 {ECO:0000313|EMBL:OMP31361.1, ECO:0000313|Proteomes:UP000188854};
RN   [1] {ECO:0000313|EMBL:OMP31361.1, ECO:0000313|Proteomes:UP000188854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DI 80 {ECO:0000313|EMBL:OMP31361.1,
RC   ECO:0000313|Proteomes:UP000188854};
RA   Krishnamurthi S., Pal Y., Verma A., Sundharam S.;
RT   "Taxonomic characterization of strain DI 80 closely related to
RT   Mangrovimonas sp.";
RL   Submitted (DEC-2016) 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). {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:OMP31361.1}.
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DR   EMBL; MSDT01000003; OMP31361.1; -; Genomic_DNA.
DR   RefSeq; WP_076663085.1; NZ_MSDT01000003.1.
DR   AlphaFoldDB; A0A1V1ZGT5; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000188854; 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; 3.30.70.20; -; 1.
DR   HAMAP; MF_00916; QueG; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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; PF08331; QueG_DUF1730; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 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}; Reference proteome {ECO:0000313|Proteomes:UP000188854};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00916}.
FT   DOMAIN          173..204
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   ACT_SITE        131
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         60
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         131
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         152
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         155
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         185
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         188
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         191
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         195
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         211
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         213
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         220
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         238..239
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         238
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         241
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         245
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
SQ   SEQUENCE   307 AA;  35178 MW;  9E1F2174B28E9146 CRC64;
     MKLLQSYTKS IKNEAKRLGF LSCGISRAGF LEDEAPRLEQ WLNSNMYGEM RYMENHFDKR
     LDPTKLVEGS KSVISLLLNY FPEKTQEDTS FKLSKYAYGT DYHFVIKDKL KQLLEFINEE
     IGEVNGRAFV DSAPVLDKAW AAKSGLGWIG KNSNLLTKQV GSFYFVAELI VDLELEYDAP
     TTDHCGSCTA CIDACPTEAI VNPYVVDGSK CISYFTIELK DNIPTEFKGK FDHWMFGCDV
     CQDVCPWNRF SKPHSEPLFN PHQDLLSMTK KDWEEITEET FNKVFKKSAV KRTKLAGLKR
     NIQFLKD
//
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