TRHO_STRP4
ID TRHO_STRP4 Reviewed; 328 AA.
AC B5E5X4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 61.
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=SPG_0092;
OS Streptococcus pneumoniae serotype 19F (strain G54).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=512566;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G54;
RX PubMed=11442348; DOI=10.1089/10766290152044995;
RA Dopazo J., Mendoza A., Herrero J., Caldara F., Humbert Y., Friedli L.,
RA Guerrier M., Grand-Schenk E., Gandin C., de Francesco M., Polissi A.,
RA Buell G., Feger G., Garcia E., Peitsch M., Garcia-Bustos J.F.;
RT "Annotated draft genomic sequence from a Streptococcus pneumoniae type 19F
RT clinical isolate.";
RL Microb. Drug Resist. 7:99-125(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G54;
RA Mulas L., Trappetti C., Hakenbeck R., Iannelli F., Pozzi G., Davidsen T.M.,
RA Tettelin H., Oggioni M.;
RT "Pneumococcal beta glucoside metabolism investigated by whole genome
RT comparison.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001015; ACF56832.1; -; Genomic_DNA.
DR RefSeq; WP_001030033.1; NC_011072.1.
DR KEGG; spx:SPG_0092; -.
DR HOGENOM; CLU_038878_1_0_9; -.
DR OMA; CDTHTNC; -.
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_1000200383"
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; 37877 MW; EDC8B3F60C907D1E CRC64;
MAKDIRVLLY YLYTPIENAE QFAADHLAFC KSIGLKGRIL VADEGINGTV SGDYETTQKY
MDYVHSLPGM EELWFKIDEE SEQAFKKMFV RYKKEIVHLG LEDNDFDNDI NPLETTGAYL
SPKEFKEALL DKDTVVLDTR NDYEYDLGHF RGAIRPDIRN FREXPQWVRD NKEKFMDKRV
VVYCTGGVRC EKFSGWMVRE GYKDVGQLHG GIATYGKDPE VQGELWDGKM YVFDERIAVD
VNHVNPTIVG KDWFDGTPCE RYVNCGNPFC NRRILTSEEN EDKYLRGCSH ECRVHPRNRY
VSKNELTQAE VIERLAAIGE SLDQAATV