TRHO_STRPZ
ID TRHO_STRPZ Reviewed; 328 AA.
AC B5XL29;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 62.
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=Spy49_0726;
OS Streptococcus pyogenes serotype M49 (strain NZ131).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=471876;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZ131;
RX PubMed=18820018; DOI=10.1128/jb.00672-08;
RA McShan W.M., Ferretti J.J., Karasawa T., Suvorov A.N., Lin S., Qin B.,
RA Jia H., Kenton S., Najar F., Wu H., Scott J., Roe B.A., Savic D.J.;
RT "Genome sequence of a nephritogenic and highly transformable M49 strain of
RT Streptococcus pyogenes.";
RL J. Bacteriol. 190:7773-7785(2008).
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; CP000829; ACI61041.1; -; Genomic_DNA.
DR RefSeq; WP_010922187.1; NC_011375.1.
DR AlphaFoldDB; B5XL29; -.
DR SMR; B5XL29; -.
DR EnsemblBacteria; ACI61041; ACI61041; Spy49_0726.
DR KEGG; soz:Spy49_0726; -.
DR HOGENOM; CLU_038878_1_0_9; -.
DR OMA; CDTHTNC; -.
DR Proteomes; UP000001039; 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 PANTHER; PTHR43268; PTHR43268; 1.
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; tRNA processing.
FT CHAIN 1..328
FT /note="tRNA uridine(34) hydroxylase"
FT /id="PRO_1000200384"
FT DOMAIN 130..224
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT ACT_SITE 184
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ SEQUENCE 328 AA; 38213 MW; 0E59DEA07D8B47A3 CRC64;
MSEKIRVLLY YKYVSIENAQ EYAAKHLEFC KSIGLKGRIL IADEGINGTV SGDYETTQKY
MDWVHSDERF ADLWFKIDEE NQQAFRKMFV RYKKEIVHLG LEDNNFDSDI NPLETTGEYL
NPKQFKEALL DEDTVVLDTR NDYEYDLGHF RGAIRPDIRN FRELPQWVRD NKDKFMEKRV
VVYCTGGVRC EKFSGWMVRE GFKDVGQLHG GIATYGKDPE VQGELWDGAM YVFDDRISVP
INHVNPTVIS KDYFDGTPCE RYVNCANPFC NKQIFASEEN ETKYVRGCSP ECRAHERNRY
VQENGLSRQE WAERLEAIGE SLPEFVGA