TRHO_RICPR
ID TRHO_RICPR Reviewed; 247 AA.
AC P41087;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 97.
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=RP125;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Madrid E;
RA Wood D.O.;
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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; U02603; AAA18324.1; -; Unassigned_DNA.
DR EMBL; AJ235270; CAA14594.1; -; Genomic_DNA.
DR PIR; C71722; C71722.
DR RefSeq; NP_220517.1; NC_000963.1.
DR RefSeq; WP_004597164.1; NC_000963.1.
DR AlphaFoldDB; P41087; -.
DR SMR; P41087; -.
DR STRING; 272947.RP125; -.
DR EnsemblBacteria; CAA14594; CAA14594; CAA14594.
DR GeneID; 57569253; -.
DR KEGG; rpr:RP125; -.
DR PATRIC; fig|272947.5.peg.127; -.
DR eggNOG; COG1054; Bacteria.
DR HOGENOM; CLU_038878_0_1_5; -.
DR OMA; CDTHTNC; -.
DR Proteomes; UP000002480; 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..247
FT /note="tRNA uridine(34) hydroxylase"
FT /id="PRO_0000161505"
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 247 AA; 28417 MW; 6F000B3C231158FC CRC64;
MNERITILSA YSFVNIIEPA NLIPKLLLVG KKKYIRGTIL LANEGFNSSF SGSYENVNIV
LKQLIALTGS KDVNVKINYS PVHPFQKLKV RLKREIIAMN VKDLNVDVFK GHYIEPKDWD
EFITKQNVIL IDTRNEYEID IGTFKSAINP RTETFKQFPA WVQQNHALLQ GKKIAMFCTG
GIRCEKSTSL LKSIGYNEVY HLKGGILQYL EDTHNKNNLW QGKCFVFDDR RAVADDLYPA
EGYWLHR