ID   TRHO_PECAS              Reviewed;         355 AA.
AC   Q6D6A4;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   25-MAY-2022, entry version 79.
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=ECA1781;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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=CAG74686.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX950851; CAG74686.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_039295108.1; NC_004547.2.
DR   AlphaFoldDB; Q6D6A4; -.
DR   SMR; Q6D6A4; -.
DR   STRING; 218491.ECA1781; -.
DR   EnsemblBacteria; CAG74686; CAG74686; ECA1781.
DR   GeneID; 57209508; -.
DR   KEGG; eca:ECA1781; -.
DR   PATRIC; fig|218491.5.peg.1808; -.
DR   eggNOG; COG1054; Bacteria.
DR   HOGENOM; CLU_038878_1_1_6; -.
DR   OrthoDB; 684577at2; -.
DR   Proteomes; UP000007966; 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_0000161476"
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;  40307 MW;  75C6D4ADE532E309 CRC64;
     MPVLHNRVSN EELKARMLAE TEPRTTVSFY KYFTIDDPKA FRDRLYIQLE QYKVFGRIYI
     AAEGINAQIS VPNNQFDAFK TGLFSAHPAL DQIRLNIALE DDGKSFWVLR MKVRERIVAD
     GIDDPTFNPA NVGQYLKADR VNAMADDPDT VFVDMRNHYE YEVGHFQNAL EVPSDTFREQ
     LPMAVDMLDD IRDKNIVMYC TGGIRCEKAS AYMLHHGFKN VYHVEGGIIE YARQAKAQGL
     PLKFIGKNFV FDERMGERIS DDVIAHCHQC GASCDSHTNC RNEGCHLLFI QCPSCAAKYE
     GCCSTQCQDE MKLPLEEQRA IRSGRENGMK IFNKSKGLLQ STLHIPAPAA KDNAE