ID   TRHO_LEPIN              Reviewed;         367 AA.
AC   Q8CXS1;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=LA_3128;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(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}.
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DR   EMBL; AE010300; AAN50326.1; -; Genomic_DNA.
DR   RefSeq; NP_713308.1; NC_004342.2.
DR   RefSeq; WP_000013216.1; NC_004342.2.
DR   AlphaFoldDB; Q8CXS1; -.
DR   SMR; Q8CXS1; -.
DR   STRING; 189518.LA_3128; -.
DR   EnsemblBacteria; AAN50326; AAN50326; LA_3128.
DR   GeneID; 61144301; -.
DR   KEGG; lil:LA_3128; -.
DR   PATRIC; fig|189518.3.peg.3106; -.
DR   HOGENOM; CLU_038878_1_1_12; -.
DR   InParanoid; Q8CXS1; -.
DR   OMA; CDTHTNC; -.
DR   Proteomes; UP000001408; Chromosome I.
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   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; Reference proteome; tRNA processing.
FT   CHAIN           1..367
FT                   /note="tRNA uridine(34) hydroxylase"
FT                   /id="PRO_0000161482"
FT   DOMAIN          159..253
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT   ACT_SITE        213
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ   SEQUENCE   367 AA;  42467 MW;  C1C1AA59DDF69785 CRC64;
     MANQGDFPKR TETKKRPLHN IYGKEILRKR LEEENFSRTT LSFYRYVILE NVQELRDQLY
     AEWEILGVLG RIYIAREGIN AQLSIPSHNL DFFRKNLDSR NQFKDMQFKI AVEDDSKSFL
     KLDLKIKKKI VADGLNDDAF DVTNVGKHLS AEEFNLHMED ENSIVVDVRN HYESEIGHFE
     NAILPQSDTF REELRILLEL LNGKENHKIL MYCTGGIRCE KASAWLKHHG YKDVNQLHGG
     IISYAHEVSQ KGLESKFKGK NFVFDGRLQE AIGNEVISSC HQCGAKCDRH VNCENPGCHV
     LFIQCPSCSE KFEGCCTLEC QNVLHLPKEK QKEIRKGKLN ENRFFSKSKI RPKISELYHG
     ILFKSSK