ID   TRHO_WOLTR              Reviewed;         269 AA.
AC   Q5GTP4;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=tRNA uridine(34) hydroxylase {ECO:0000255|HAMAP-Rule:MF_00469};
DE            EC=1.14.-.- {ECO:0000255|HAMAP-Rule:MF_00469};
DE   AltName: Full=tRNA hydroxylation protein O {ECO:0000255|HAMAP-Rule:MF_00469};
GN   Name=trhO {ECO:0000255|HAMAP-Rule:MF_00469}; OrderedLocusNames=Wbm0038;
OS   Wolbachia sp. subsp. Brugia malayi (strain TRS).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX   NCBI_TaxID=292805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRS;
RX   PubMed=15780005; DOI=10.1371/journal.pbio.0030121;
RA   Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N.,
RA   Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J.,
RA   Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S.,
RA   Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D.,
RA   Koonin E., Slatko B.;
RT   "The Wolbachia genome of Brugia malayi: endosymbiont evolution within a
RT   human pathogenic nematode.";
RL   PLoS Biol. 3:599-614(2005).
CC   -!- FUNCTION: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U)
CC       modification at position 34 in tRNAs. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00469};
CC   -!- SIMILARITY: Belongs to the TrhO family. {ECO:0000255|HAMAP-
CC       Rule:MF_00469}.
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DR   EMBL; AE017321; AAW70630.1; -; Genomic_DNA.
DR   RefSeq; WP_011256240.1; NC_006833.1.
DR   AlphaFoldDB; Q5GTP4; -.
DR   SMR; Q5GTP4; -.
DR   PRIDE; Q5GTP4; -.
DR   EnsemblBacteria; AAW70630; AAW70630; Wbm0038.
DR   KEGG; wbm:Wbm0038; -.
DR   eggNOG; COG1054; Bacteria.
DR   HOGENOM; CLU_038878_0_1_5; -.
DR   OMA; CDTHTNC; -.
DR   OrthoDB; 684577at2; -.
DR   Proteomes; UP000000534; Chromosome.
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   Gene3D; 3.40.250.10; -; 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; PTHR43268; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF17773; UPF0176_N; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; SSF52821; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; tRNA processing.
FT   CHAIN           1..269
FT                   /note="tRNA uridine(34) hydroxylase"
FT                   /id="PRO_0000161538"
FT   DOMAIN          121..214
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT   ACT_SITE        174
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ   SEQUENCE   269 AA;  30838 MW;  3266851303D03439 CRC64;
     MSFVIATFYH FVKLSNYYDM KDEIKAACDN FELKGTILLA EEGINATISG ERNAINKIFN
     FLCSDYRLKD LTWKESAAKY QPFSKMKVRL KREIVNLGVS NLDTSLRGKY IDPDHWDDFI
     SQPDVLVIDT RNEYEVKLGK FKNAINPYIQ YFREFPQWAK SFSKNKNLKV AMYCTGGIRC
     EKSTAYMKSL GFNDVYHLKG GILSYLERTH NKNGNWEGEC FVFDDRIAIN SSLAPSNKIK
     CIFCSNQVSA DELKSVSRGQ VVCSDCNPS