TRHO_LEGPL
ID TRHO_LEGPL Reviewed; 254 AA.
AC Q5WSX6;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=lpl2750;
OS Legionella pneumophila (strain Lens).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lens;
RX PubMed=15467720; DOI=10.1038/ng1447;
RA Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA Glaser P., Buchrieser C.;
RT "Evidence in the Legionella pneumophila genome for exploitation of host
RT cell functions and high genome plasticity.";
RL Nat. Genet. 36:1165-1173(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}.
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DR EMBL; CR628337; CAH16993.1; -; Genomic_DNA.
DR RefSeq; WP_011216673.1; NC_006369.1.
DR AlphaFoldDB; Q5WSX6; -.
DR SMR; Q5WSX6; -.
DR EnsemblBacteria; CAH16993; CAH16993; lpl2750.
DR KEGG; lpf:lpl2750; -.
DR LegioList; lpl2750; -.
DR HOGENOM; CLU_038878_0_1_6; -.
DR OMA; CDTHTNC; -.
DR Proteomes; UP000002517; 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..254
FT /note="tRNA uridine(34) hydroxylase"
FT /id="PRO_0000161485"
FT DOMAIN 123..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 254 AA; 29936 MW; F0B01F16D0DCE0EE CRC64;
MKDIIIASFY KFIPLNDFES LREPILTKMH EIGIKGTIIL AHEGVNGGFA GNREQMYIFY
DYLRSDSRFA DLHFKETYDN KNPFDKAKVK LRKEIVTMGV QKVDPSYNAG TYLSPEEWHQ
FIQDPNVILL DTRNDYEYEL GTFKNAINPD IENFREFPDY VQRNLIDKKD KKIAMFCTGG
IRCEKTTAYM KELGFQHVYQ LHDGILNYLE SIPEGESLWE GKCFVFDDRV AVDQKLDRVY
PQLPQDYKYE REQK