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Database: UniProt
Entry: D0KZJ3_HALNC
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Original site: D0KZJ3_HALNC 
ID   D0KZJ3_HALNC            Unreviewed;       373 AA.
AC   D0KZJ3;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   28-FEB-2018, entry version 49.
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   OrderedLocusNames=Hneap_1030 {ECO:0000313|EMBL:ACX95866.1};
OS   Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus
OS   neapolitanus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Halothiobacillaceae; Halothiobacillus.
OX   NCBI_TaxID=555778 {ECO:0000313|EMBL:ACX95866.1, ECO:0000313|Proteomes:UP000009102};
RN   [1] {ECO:0000313|EMBL:ACX95866.1, ECO:0000313|Proteomes:UP000009102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23641 / c2 {ECO:0000313|Proteomes:UP000009102};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Davenport K., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Kerfeld C., Cannon G., Heinhort S.;
RT   "Complete sequence of Halothiobacillus neapolitanus c2.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of epoxyqueuosine (oQ) to
CC       queuosine (Q), which is a hypermodified base found in the wobble
CC       positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
CC       {ECO:0000256|HAMAP-Rule:MF_00916}.
CC   -!- CATALYTIC ACTIVITY: Queuosine(34) in tRNA + acceptor + H(2)O =
CC       epoxyqueuosine(34) in tRNA + reduced acceptor. {ECO:0000256|HAMAP-
CC       Rule:MF_00916}.
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {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}.
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DR   EMBL; CP001801; ACX95866.1; -; Genomic_DNA.
DR   RefSeq; WP_012823902.1; NC_013422.1.
DR   STRING; 555778.Hneap_1030; -.
DR   EnsemblBacteria; ACX95866; ACX95866; Hneap_1030.
DR   KEGG; hna:Hneap_1030; -.
DR   eggNOG; ENOG4105EH2; Bacteria.
DR   eggNOG; COG1600; LUCA.
DR   HOGENOM; HOG000272643; -.
DR   KO; K18979; -.
DR   OMA; VDGSKCI; -.
DR   OrthoDB; POG091H01VA; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000009102; Chromosome.
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: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_00916; QueG; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR013542; DUF1730.
DR   InterPro; IPR004453; QueG.
DR   PANTHER; PTHR30002; PTHR30002; 1.
DR   Pfam; PF08331; DUF1730; 1.
DR   TIGRFAMs; TIGR00276; TIGR00276; 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   Complete proteome {ECO:0000313|Proteomes:UP000009102};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00916};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009102};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   DOMAIN      179    211       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   METAL       191    191       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   METAL       194    194       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   METAL       197    197       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   METAL       201    201       Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00916}.
FT   METAL       244    244       Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00916}.
FT   METAL       247    247       Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00916}.
FT   METAL       251    251       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
SQ   SEQUENCE   373 AA;  41919 MW;  827E5B8871B9A5E3 CRC64;
     MFNPDELKAQ IKVWAIELGF DELRVTDTDL SHYEAGYLDW IAQKHQGTMD YLVTHGLKRF
     RPAELVPGTL RVLAVRKNYL PPDSSGPRDV LHNPELGYVS RYALGRDYHK VMRSNLQKLA
     ERITQEIGAF GFRAFVDSAP VYETGLAEKA GIGWKGKHSL ILNRQGGSWF FLGELFIDFD
     LPVDEPVESH CGSCTACITV CPTQAIVADG VVDARRCISY LTIESKDDIP PEFREAMGNR
     IYGCDDCQLV CPWNRFARVA ADADFRARHG LDAPGLIELF LWDEPTFLHK TEGMAIRRIG
     WQRWLRNVAV ALGNLLRNQP DNTSAVAALQ ARCGQVGDQL DRHIQWALAQ REGLPNGESK
     TAKMFEDALS MPE
//
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