GenomeNet

Database: UniProt
Entry: A0A135W338_9BACL
LinkDB: A0A135W338_9BACL
Original site: A0A135W338_9BACL 
ID   A0A135W338_9BACL        Unreviewed;       385 AA.
AC   A0A135W338;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=AU377_12110 {ECO:0000313|EMBL:KXH79317.1};
OS   Sporosarcina sp. HYO08.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX   NCBI_TaxID=1759557 {ECO:0000313|EMBL:KXH79317.1, ECO:0000313|Proteomes:UP000070230};
RN   [1] {ECO:0000313|EMBL:KXH79317.1, ECO:0000313|Proteomes:UP000070230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HYO08 {ECO:0000313|EMBL:KXH79317.1,
RC   ECO:0000313|Proteomes:UP000070230};
RA   Choi I.-G., Park W.;
RT   "Draft genome sequences of microorganisms having biocementation activity.";
RL   Submitted (DEC-2015) 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:KXH79317.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LPUT01000029; KXH79317.1; -; Genomic_DNA.
DR   RefSeq; WP_067408385.1; NZ_LPUT01000029.1.
DR   AlphaFoldDB; A0A135W338; -.
DR   STRING; 1759557.AU377_12110; -.
DR   OrthoDB; 9784571at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000070230; 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   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}; Reference proteome {ECO:0000313|Proteomes:UP000070230};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00916}.
FT   DOMAIN          178..208
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   ACT_SITE        134
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         57
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         97
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         134
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         139..141
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         158
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         169
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
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         194
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         198
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         214
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         216
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         222
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         240..241
FT                   /ligand="cob(II)alamin"
FT                   /ligand_id="ChEBI:CHEBI:16304"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         240
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         243
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         247
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         281
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         282
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         296
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
FT   BINDING         298
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00916"
SQ   SEQUENCE   385 AA;  43367 MW;  0E158F1E8673D4E3 CRC64;
     MNAVRLQREL REYAQSIGID KIGFTTAAPF RELKNRLKRQ QELGYQSGFE EKDLEKRTEP
     ARLLDQAESI IAIAIAYPTK IENAPKGKKN ERRGIFCRAS WGTDYHIVLR EKLALLEQFI
     YERVPEAKLR SMVDTGELSD RAVAERAGIG WSGKNCSIIT PEFGSYVYLG EMITNIPFAP
     DVPLEDECGD CRLCLDACPT GALIQGGQIN AQRCISFLTQ TKTTIPEEFR AKIGNRVYGC
     DTCQTVCPKN KRKHNLHRTE TFEPDPELAK PLLQPILQLS NRQFKEQFGQ VAGSWRGKNP
     IQRNAIIAIG HFKDESAVPM LNNLLQEDPR PVIRGTIAWA LGEISSEASK QAIDAALVTE
     QEPDVRAELL KARSNWKEKV GELRK
//
DBGET integrated database retrieval system