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Database: UniProt
Entry: A0A0M2REH6_9PROT
LinkDB: A0A0M2REH6_9PROT
Original site: A0A0M2REH6_9PROT 
ID   A0A0M2REH6_9PROT        Unreviewed;       379 AA.
AC   A0A0M2REH6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   28-FEB-2018, entry version 15.
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=WH95_03805 {ECO:0000313|EMBL:KKJ78420.1};
OS   Kiloniella litopenaei.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Kiloniellales;
OC   Kiloniellaceae; Kiloniella.
OX   NCBI_TaxID=1549748 {ECO:0000313|EMBL:KKJ78420.1, ECO:0000313|Proteomes:UP000034491};
RN   [1] {ECO:0000313|EMBL:KKJ78420.1, ECO:0000313|Proteomes:UP000034491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1-1 {ECO:0000313|EMBL:KKJ78420.1,
RC   ECO:0000313|Proteomes:UP000034491};
RA   Shao Z., Wang L., Li X.;
RT   "Genome sequence of Kiloniella sp. P1-1, isolated from the gut
RT   microflora of Pacific white shrimp, Penaeus vannamei.";
RL   Submitted (MAR-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KKJ78420.1}.
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DR   EMBL; LANI01000002; KKJ78420.1; -; Genomic_DNA.
DR   RefSeq; WP_046503036.1; NZ_LANI01000002.1.
DR   EnsemblBacteria; KKJ78420; KKJ78420; WH95_03805.
DR   PATRIC; fig|1549748.8.peg.1369; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000034491; 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: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; -; 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; 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   SUPFAM; SSF48371; SSF48371; 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:UP000034491};
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:UP000034491};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   DOMAIN      188    217       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   METAL       197    197       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   METAL       200    200       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   METAL       203    203       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
FT   METAL       207    207       Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00916}.
FT   METAL       250    250       Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00916}.
FT   METAL       253    253       Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00916}.
FT   METAL       257    257       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00916}.
SQ   SEQUENCE   379 AA;  43107 MW;  91E58416EDC1B216 CRC64;
     MSKKSKQSSA SLLDPASAIR EKALELKFNT VGFSPAKINE KNQKNLRTFL DLGYHGDMAW
     MENRIEWRED PTAMWEDAKS IIVLGVNYGP AEPALANLDF DDRGNISVYA RNKDYHDFIK
     KRLKALARWM VENLGCQVKV FVDTAPVLEK VAAAQSGIGW QGKNTHLVSR EYGSWLFLGE
     IYTDLDLKTD RHEEDHCGSC NKCLSICPTD AFPSPYVLDA KRCISYLTIE YHGHIAEEFR
     APMGNRIYGC DDCIAICPWN KFAEVTTEEH VFPRIELTAP RLADLAELDD ATFRQVFSGS
     PVKRIGRDRF IRNVLIGIGN CGDKSIVKRI TPLLKDSSPY VRAMAVWAMK RLLDKQEFED
     LKLEYKDDEP DADVLVEWL
//
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