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Database: UniProt
Entry: K2BV15_9BACT
LinkDB: K2BV15_9BACT
Original site: K2BV15_9BACT 
ID   K2BV15_9BACT            Unreviewed;       277 AA.
AC   K2BV15;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   22-FEB-2023, entry version 31.
DE   RecName: Full=tRNA uridine(34) hydroxylase {ECO:0000256|HAMAP-Rule:MF_00469};
DE            EC=1.14.-.- {ECO:0000256|HAMAP-Rule:MF_00469};
DE   AltName: Full=tRNA hydroxylation protein O {ECO:0000256|HAMAP-Rule:MF_00469};
GN   Name=trhO {ECO:0000256|HAMAP-Rule:MF_00469};
GN   ORFNames=ACD_42C00160G0002 {ECO:0000313|EMBL:EKD77842.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD77842.1};
RN   [1] {ECO:0000313|EMBL:EKD77842.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
CC   -!- FUNCTION: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U)
CC       modification at position 34 in tRNAs. {ECO:0000256|HAMAP-
CC       Rule:MF_00469}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA
CC         + A + H2O; Xref=Rhea:RHEA:64224, Rhea:RHEA-COMP:11727, Rhea:RHEA-
CC         COMP:13381, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:65315, ChEBI:CHEBI:136877;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00469};
CC   -!- SIMILARITY: Belongs to the TrhO family. {ECO:0000256|HAMAP-
CC       Rule:MF_00469}.
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:EKD77842.1}.
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DR   EMBL; AMFJ01017431; EKD77842.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2BV15; -.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProtKB-UniRule.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   CDD; cd01518; RHOD_YceA; 1.
DR   Gene3D; 3.30.70.100; -; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   HAMAP; MF_00469; TrhO; 1.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR020936; TrhO.
DR   InterPro; IPR040503; TRHO_N.
DR   PANTHER; PTHR43268:SF3; RHODANESE-LIKE DOMAIN-CONTAINING PROTEIN 7-RELATED; 1.
DR   PANTHER; PTHR43268; THIOSULFATE SULFURTRANSFERASE/RHODANESE-LIKE DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF17773; UPF0176_N; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00469};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00469}.
FT   DOMAIN          128..222
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   277 AA;  31417 MW;  87CA5801C6D4F67A CRC64;
     MNQLPIVNLS GYRFVSLKEA QLPQMRVDIK TKAAECNLKG TILLSREGIN AFLAGTRENS
     DAFVNYLRNI PEFANLHFKE SFTDYQPFNR MLVRLKKEII PMNKENVNPE KKTAPYVSPE
     ELKQWYAEKR DMIVLDTRND FEVALGTFEN AVDLHIAHFR EFNDAVDLLP PESKEKTVVT
     FCTGGIRCEK AAELMAQKGF KNVYQLDGGI LNYFEKCGGD FYNGECFVFD QRVAVNSALQ
     ETDAKQCFDC RTPLQNNAIK DGKCPHCGSK SISKQAA
//
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