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Database: UniProt
Entry: A0A0R2XTN5_9BACT
LinkDB: A0A0R2XTN5_9BACT
Original site: A0A0R2XTN5_9BACT 
ID   A0A0R2XTN5_9BACT        Unreviewed;       278 AA.
AC   A0A0R2XTN5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   28-JUN-2023, entry version 24.
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=ABS34_05895 {ECO:0000313|EMBL:KRP36766.1};
OS   Opitutaceae bacterium BACL24 MAG-120322-bin51.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX   NCBI_TaxID=1655636 {ECO:0000313|EMBL:KRP36766.1, ECO:0000313|Proteomes:UP000054041};
RN   [1] {ECO:0000313|EMBL:KRP36766.1, ECO:0000313|Proteomes:UP000054041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL24 MAG-120322-bin51 {ECO:0000313|EMBL:KRP36766.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA   Andersson A.F.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KRP36766.1}.
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DR   EMBL; LIDO01000054; KRP36766.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2XTN5; -.
DR   Proteomes; UP000054041; Unassembled WGS sequence.
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          124..218
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   278 AA;  31690 MW;  A13FA4FE4DCF0EA7 CRC64;
     MSESWKIAAF YHFVDLPDRD EWAERLIDHG LQVGLRGTVI FASEGINSTC AGSHEAVDAT
     IALLKSDPRF AAMEVKVSYA DFCPFPKFKV KKKPEIVTFR QDGADPRDEV GTYLDPDEWN
     ELISDPDVIT IDTRNDYEVG VGKFKGAINP DTDDFTEFAK FVDEHLTAQK DKKIAMYCTG
     GIRCERSTAY LKQKGFTNVY HLKGGILRYM ELMPKETSLW EGDCFVFDYR VALDHDLKPA
     KWKIDPETSF PARMNEEDVE RIAERRRSGA IFKKPYAG
//
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