ID   TRHO_STRPQ              Reviewed;         328 AA.
AC   P0DG91; Q8K7U2;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   25-MAY-2022, entry version 40.
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=SPs1223;
OS   Streptococcus pyogenes serotype M3 (strain SSI-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=193567;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSI-1;
RX   PubMed=12799345; DOI=10.1101/gr.1096703;
RA   Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA   Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA   Hattori M., Hamada S.;
RT   "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT   scale genomic rearrangement in invasive strains and new insights into phage
RT   evolution.";
RL   Genome Res. 13:1042-1055(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC64318.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000034; BAC64318.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011054391.1; NC_004606.1.
DR   AlphaFoldDB; P0DG91; -.
DR   SMR; P0DG91; -.
DR   KEGG; sps:SPs1223; -.
DR   HOGENOM; CLU_1776293_0_0_9; -.
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; IPR022111; Rhodanese_C.
DR   InterPro; IPR020936; TrhO.
DR   InterPro; IPR040503; TRHO_N.
DR   PANTHER; PTHR43268; PTHR43268; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF12368; Rhodanese_C; 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..328
FT                   /note="tRNA uridine(34) hydroxylase"
FT                   /id="PRO_0000411635"
FT   DOMAIN          130..224
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT   ACT_SITE        184
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ   SEQUENCE   328 AA;  38199 MW;  F4E518DAC15B47BB CRC64;
     MSEKIRVLLY YKYVSIENAQ EYAAKHLEFC KSIGLKGRIL IADEGINGTV SGDYETTQKY
     MDWVHSDERF ADLWFKIDEE NQQAFRKMFV RYKKEIVHLG LEDNNFDSDI NPLETTGEYL
     NPKQFKEALL DEDTVVLDTR NDYEYDLGHF RGAIRPDIRN FRELPQWVRD NKDKFMEKRV
     VVYCTGGVRC EKFSGWMVRE GFKDVGQLHG GIATYGKDPE VQGELWDGAM YVFDDRISVP
     INHVNPTVVS KDYFDGTPCE RYVNCANPFC NKQIFASEEN ETKYVRGCSP ECRAHERNRY
     VQENGLSRQE WAERLEAIGE SLPEFVGA