ID   TRHO_PSEPK              Reviewed;         310 AA.
AC   Q88M17;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=PP_1758;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN67378.1; -; Genomic_DNA.
DR   RefSeq; NP_743914.1; NC_002947.4.
DR   RefSeq; WP_010952798.1; NC_002947.4.
DR   AlphaFoldDB; Q88M17; -.
DR   SMR; Q88M17; -.
DR   STRING; 160488.PP_1758; -.
DR   EnsemblBacteria; AAN67378; AAN67378; PP_1758.
DR   KEGG; ppu:PP_1758; -.
DR   PATRIC; fig|160488.4.peg.1853; -.
DR   eggNOG; COG1054; Bacteria.
DR   HOGENOM; CLU_038878_0_0_6; -.
DR   OMA; CDTHTNC; -.
DR   PhylomeDB; Q88M17; -.
DR   BioCyc; PPUT160488:G1G01-1859-MON; -.
DR   Proteomes; UP000000556; 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; Reference proteome; tRNA processing.
FT   CHAIN           1..310
FT                   /note="tRNA uridine(34) hydroxylase"
FT                   /id="PRO_0000161498"
FT   DOMAIN          124..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   310 AA;  35163 MW;  299D30788FE1791B CRC64;
     MSQAIVVAAL YKFVTLEDYV ELREPLLKTM LDNNVKGTLL LAQEGINGTV SGTREGIDGL
     LAWLRSDPRL VDIDHKESYC DEQPFYRTKV KLKKEIVTLG VPGVDPNKAV GTYVEPKDWN
     ALISDPEVLL IDTRNDYEVA IGTFKGAIDP KTETFREFPE YIKANFDPSK HKKVAMFCTG
     GIRCEKASSY MLGEGFESVY HLKGGILKYF EEVPQEESLW DGDCFVFDNR VTVRHDLSEG
     EYDQCHACRH PINAQERASE HYSPGVSCPH CWDSLSEKTR RSAIDRQKQI ELAKARNLPH
     PIGYYYKAEA