ID   TRHO_CHLTR              Reviewed;         327 AA.
AC   O84632;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=CT_627;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC68231.1; -; Genomic_DNA.
DR   PIR; D71491; D71491.
DR   RefSeq; NP_220144.1; NC_000117.1.
DR   RefSeq; WP_009871996.1; NC_000117.1.
DR   AlphaFoldDB; O84632; -.
DR   SMR; O84632; -.
DR   STRING; 272561.CT_627; -.
DR   EnsemblBacteria; AAC68231; AAC68231; CT_627.
DR   GeneID; 884407; -.
DR   KEGG; ctr:CT_627; -.
DR   PATRIC; fig|272561.5.peg.686; -.
DR   HOGENOM; CLU_038878_1_0_0; -.
DR   InParanoid; O84632; -.
DR   OMA; CDTHTNC; -.
DR   Proteomes; UP000000431; 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; Reference proteome; tRNA processing.
FT   CHAIN           1..327
FT                   /note="tRNA uridine(34) hydroxylase"
FT                   /id="PRO_0000161465"
FT   DOMAIN          122..218
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT   ACT_SITE        178
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ   SEQUENCE   327 AA;  37694 MW;  3A2E687393920432 CRC64;
     MEKNYYALAY YYFGPVSNPH EEIALHKQLF KTMDVSCRIY ISEEGINGQF SGYQPDAERY
     MAWLKQRPDF ASIKFKIHHI EENIFPRVTV KYRKELVALG CSVDTTKQGK HISPEEWHEK
     LQENRCLVLD VRNNYEWKIG HFENAVLPDI ETFREFPDYA DRLAKEHDPA KTPVMMYCTG
     GIRCELYSAL LLEKGFKEVY QLDGGVIAYG LKMGTGKWRG KLFVFDDRMA MPIDEADPNV
     SPIARCSLCN TDSDTYYNCA NTDCNNLFIC CESCIATHKG CCSEECSQAP RIRAFSAERG
     NKPFRRKHLC PTIEQSCCLK EQENQPA