ID   TRHO_EHRRW              Reviewed;         272 AA.
AC   Q5HBX1; Q5FCZ9;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-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};
GN   OrderedLocusNames=Erum2040, ERWE_CDS_02060;
OS   Ehrlichia ruminantium (strain Welgevonden).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=254945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Welgevonden;
RX   PubMed=15637156; DOI=10.1073/pnas.0406633102;
RA   Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E.,
RA   Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M.,
RA   Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C.,
RA   Berthier D., Botha M., Joubert F., Corton C.H., Thomson N.R., Allsopp M.T.,
RA   Allsopp B.A.;
RT   "The genome of the heartwater agent Ehrlichia ruminantium contains multiple
RT   tandem repeats of actively variable copy number.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Welgevonden;
RX   PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA   Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA   Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT   "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT   reveals an active process of genome size plasticity.";
RL   J. Bacteriol. 188:2533-2542(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI26700.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CR767821; CAH57922.1; -; Genomic_DNA.
DR   EMBL; CR925678; CAI26700.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; WP_011154890.1; NC_005295.2.
DR   AlphaFoldDB; Q5HBX1; -.
DR   SMR; Q5HBX1; -.
DR   STRING; 254945.Erum2040; -.
DR   EnsemblBacteria; CAI26700; CAI26700; ERWE_CDS_02060.
DR   KEGG; eru:Erum2040; -.
DR   KEGG; erw:ERWE_CDS_02060; -.
DR   eggNOG; COG1054; Bacteria.
DR   HOGENOM; CLU_038878_0_1_5; -.
DR   OMA; CDTHTNC; -.
DR   BioCyc; ERUM254945:ERUM_RS01140-MON; -.
DR   Proteomes; UP000001021; 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..272
FT                   /note="tRNA uridine(34) hydroxylase"
FT                   /id="PRO_0000161474"
FT   DOMAIN          121..217
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT   ACT_SITE        177
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ   SEQUENCE   272 AA;  31254 MW;  C6FE9EFE5F6ED671 CRC64;
     MGYVVSTFYR FVHLSNYYDI RPVLKEFCVQ NNIKGTIILA EQGINATIAG SQNSLDKFFS
     FLDLDSRLCN LQYHKSFSRC NPFSKMKVKL RKELVCLGIE DFDDSVGGEY IDPENWDNFI
     SRSDVYTIDT RNSYEINFGK FKNSINPETN CFRDFPDWAI SWAKNKIDDD PIIAMYCTGG
     IRCEKSTAFM KDLGFSKVYH LKGGILEYFK STGNINNLWE GYCFTFDDRI IVDDKLVPGD
     VKCILCGAHV MLEDMKSISR GHVLCFSCKD HV