ID   TRHO_STRPF              Reviewed;         328 AA.
AC   Q1J713;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 76.
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};
GN   OrderedLocusNames=MGAS10750_Spy0811;
OS   Streptococcus pyogenes serotype M4 (strain MGAS10750).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS10750;
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA   Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in the
RT   human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000262; ABF37761.1; -; Genomic_DNA.
DR   RefSeq; WP_010922187.1; NC_008024.1.
DR   AlphaFoldDB; Q1J713; -.
DR   SMR; Q1J713; -.
DR   PRIDE; Q1J713; -.
DR   EnsemblBacteria; ABF37761; ABF37761; MGAS10750_Spy0811.
DR   KEGG; spi:MGAS10750_Spy0811; -.
DR   HOGENOM; CLU_038878_1_0_9; -.
DR   OMA; CDTHTNC; -.
DR   Proteomes; UP000002434; 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; 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_1000013787"
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;  38213 MW;  0E59DEA07D8B47A3 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
     INHVNPTVIS KDYFDGTPCE RYVNCANPFC NKQIFASEEN ETKYVRGCSP ECRAHERNRY
     VQENGLSRQE WAERLEAIGE SLPEFVGA