ID A0A0C4Y5G7_9BURK Unreviewed; 371 AA.
AC A0A0C4Y5G7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 25-OCT-2017, entry version 13.
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=RR42_m0701 {ECO:0000313|EMBL:AJG18113.1};
OS Cupriavidus basilensis.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG18113.1, ECO:0000313|Proteomes:UP000031843};
RN [1] {ECO:0000313|EMBL:AJG18113.1, ECO:0000313|Proteomes:UP000031843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G11 {ECO:0000313|EMBL:AJG18113.1};
RX PubMed=25977418;
RA Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA Chakraborty R., Arkin A.P., Deutschbauer A.;
RT "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated
RT from the Oak Ridge Field Research Center Site.";
RL Genome Announc. 3:0-0(2015).
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; CP010536; AJG18113.1; -; Genomic_DNA.
DR EnsemblBacteria; AJG18113; AJG18113; RR42_m0701.
DR KEGG; cbw:RR42_m0701; -.
DR KO; K18979; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000031843; Chromosome main.
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:UP000031843};
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:UP000031843};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00916}.
FT DOMAIN 193 222 4Fe-4S ferredoxin-type.
FT {ECO:0000259|PROSITE:PS51379}.
FT METAL 202 202 Iron-sulfur 1 (4Fe-4S).
FT {ECO:0000256|HAMAP-Rule:MF_00916}.
FT METAL 205 205 Iron-sulfur 1 (4Fe-4S).
FT {ECO:0000256|HAMAP-Rule:MF_00916}.
FT METAL 208 208 Iron-sulfur 1 (4Fe-4S).
FT {ECO:0000256|HAMAP-Rule:MF_00916}.
FT METAL 212 212 Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT MF_00916}.
FT METAL 255 255 Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT MF_00916}.
FT METAL 258 258 Iron-sulfur 2. {ECO:0000256|HAMAP-Rule:
FT MF_00916}.
FT METAL 262 262 Iron-sulfur 1 (4Fe-4S).
FT {ECO:0000256|HAMAP-Rule:MF_00916}.
SQ SEQUENCE 371 AA; 40408 MW; 48A0C5EE45D037B6 CRC64;
MHAGTDAAGL EALVGSIRAW GTELGFDALS IADVDLSRAE AGLLAWLAQG YHGDMDYMAN
HGLRRARPAE LVPGTVRAIV ARMPYLSAAG PHDWRAHELA RLDDPATAVV SLYARGRDYH
KVLRNRLQQL ASRIEAAIGP FGYRVFTDSA PVMEVALAAQ GGLGWRGKHT LLLDRDGGSM
FFLGEILVDV PFPADAPEPG HCGNCRRCID ICPTQAILEP YRIDARRCIS YLTIEHKGAI
PEALRAPMGN RVYGCDDCQL ACPWNKFAHR ATLPDFDVRN GLDAPDMAEL FGWTQAQFNQ
RLEGSPIRRI GHERWLRNLA VGLGNSLRAA VASGDTALAT RIRAALGARQ AEASPLVREH
IDWALAQAPA N
//
