ID   TRHO_HAMD5              Reviewed;         355 AA.
AC   C4K8L9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 60.
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=HDEF_0081;
OS   Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts; Candidatus Hamiltonella.
OX   NCBI_TaxID=572265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5AT;
RX   PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA   Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT   "Hamiltonella defensa, genome evolution of protective bacterial
RT   endosymbiont from pathogenic ancestors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009).
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; CP001277; ACQ66856.1; -; Genomic_DNA.
DR   RefSeq; WP_012737821.1; NC_012751.1.
DR   AlphaFoldDB; C4K8L9; -.
DR   SMR; C4K8L9; -.
DR   STRING; 572265.HDEF_0081; -.
DR   EnsemblBacteria; ACQ66856; ACQ66856; HDEF_0081.
DR   GeneID; 66260022; -.
DR   KEGG; hde:HDEF_0081; -.
DR   eggNOG; COG1054; Bacteria.
DR   HOGENOM; CLU_038878_1_1_6; -.
DR   OMA; CDTHTNC; -.
DR   Proteomes; UP000002334; 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   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..355
FT                   /note="tRNA uridine(34) hydroxylase"
FT                   /id="PRO_1000206336"
FT   DOMAIN          146..240
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT   ACT_SITE        200
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ   SEQUENCE   355 AA;  41135 MW;  9862664101A8C06C CRC64;
     MPVLHNRISN QKLKEKMLAE TQERQTLSFY KYFALDNPSM FRDKLYTQWN QLSVFGRVYI
     AKEGINAQIS VPIDHYNDFK ASLFNAHPAL DQIRLNTALE DNGRSFWVLR MKVRQRIVAD
     GIEDETFNPA HTGQYLKAHE VNEMIKDPDA LFVDMRNHYE YEVGHFKNAI KVPSDTFREQ
     LPMAVDMLKE DKEKKMVLYC TGGIRCEKAS AYLLHHGFKN VYHVEGGIIE YVRTAKKKDL
     PLHFIGKNFV FDERMGERVS EEVIAHCHQC EQFCDTHVNC HNSACHLLFI QCAICSEKFS
     GCCSAICQEE LELSPEEQRL RRSARGNKIK IFNKSKDVLE TIMNKSIIDQ GNKEG