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Database: UniProt
Entry: H1Z5V4_MYROD
LinkDB: H1Z5V4_MYROD
Original site: H1Z5V4_MYROD 
ID   H1Z5V4_MYROD            Unreviewed;       307 AA.
AC   H1Z5V4;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   25-OCT-2017, entry version 32.
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=Myrod_2272 {ECO:0000313|EMBL:EHQ43098.1};
OS   Myroides odoratus DSM 2801.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Myroides.
OX   NCBI_TaxID=929704 {ECO:0000313|EMBL:EHQ43098.1, ECO:0000313|Proteomes:UP000005785};
RN   [1] {ECO:0000313|EMBL:EHQ43098.1, ECO:0000313|Proteomes:UP000005785}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2801 {ECO:0000313|EMBL:EHQ43098.1,
RC   ECO:0000313|Proteomes:UP000005785};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N.,
RA   Lu M., Kyrpides N., Mavromatis K., Ivanova N., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The draft genome of Myroides odoratus DSM 2801.";
RL   Submitted (OCT-2011) 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; CM001437; EHQ43098.1; -; Genomic_DNA.
DR   RefSeq; WP_002989862.1; NZ_CM001437.1.
DR   EnsemblBacteria; EHQ43098; EHQ43098; Myrod_2272.
DR   OrthoDB; POG091H01VA; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000005785; 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; IPR009051; Helical_ferredxn.
DR   InterPro; IPR004453; QueG.
DR   PANTHER; PTHR30002; PTHR30002; 1.
DR   Pfam; PF08331; DUF1730; 1.
DR   SUPFAM; SSF46548; SSF46548; 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:UP000005785};
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:UP000005785};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   DOMAIN      176    205       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   METAL       185    185       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   METAL       188    188       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   METAL       191    191       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   METAL       195    195       Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00916}.
FT   METAL       238    238       Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00916}.
FT   METAL       241    241       Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00916}.
FT   METAL       245    245       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
SQ   SEQUENCE   307 AA;  34825 MW;  26F66C074AB6AD01 CRC64;
     MDKKSHYAAL IKAEAKRLGF LSCGISEAGF LEEEAPRLEK WLNANMHGSM QYMENHFDKR
     LNPTLLVEGA KSVVSLLFNY YPEQEQTDGA YKISKYAYGE DYHYVVKDKL KELLHFIHDN
     IGAVDGRAFV DSAPILDKAW AAKSGLGWVG KNSNLISKQV GSFFFIAELI IDLELESDGA
     TTDHCGKCTR CIDACPTGAI ESAYIVNGSK CISYFTIELK DDIPAELAGQ FDNWMYGCDV
     CQDVCPWNRF AKPHNEPRFT PNEALMNYSN KEWEELTNEV FNDIFRKSAV KRTKYTGLVR
     NIKFLKE
//
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