TRHO_EHRRG
ID TRHO_EHRRG Reviewed; 272 AA.
AC Q5FFG3;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=ERGA_CDS_02010;
OS Ehrlichia ruminantium (strain Gardel).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=302409;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gardel;
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}.
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DR EMBL; CR925677; CAI27653.1; -; Genomic_DNA.
DR RefSeq; WP_011255373.1; NC_006831.1.
DR AlphaFoldDB; Q5FFG3; -.
DR SMR; Q5FFG3; -.
DR EnsemblBacteria; CAI27653; CAI27653; ERGA_CDS_02010.
DR KEGG; erg:ERGA_CDS_02010; -.
DR HOGENOM; CLU_038878_0_1_5; -.
DR OMA; CDTHTNC; -.
DR OrthoDB; 684577at2; -.
DR BioCyc; ERUM302409:ERGA_RS01060-MON; -.
DR Proteomes; UP000000533; 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_0000161473"
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; 31283 MW; 8D533DFFCCA596C1 CRC64;
MGYVVSTFYR FVHLSNYYDI RPVLKEFCVQ NNIKGTIILA EQGINATIAG SQNSLDKFFS
FLDLDSRLCN LQYHKSFSRC NPFSKMKVKL RKELVCLGIE DFDNSVSGEY IDPENWDNFI
SRSDVYTIDT RNSYEINFGK FKNSINPETN CFRDFPDWAI SWAKNKIDDD PIIAMYCTGG
IRCEKSTAFM KDLGFSKVYH LKGGILEYFK STGNINNLWE GYCFTFDDRI IVDDKLVPGD
VKCILCGAHV MLEDMKSISR GHVLCFSCKD HV