ID T0VAW4_9STRE Unreviewed; 327 AA.
AC T0VAW4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=tRNA uridine(34) hydroxylase {ECO:0000256|HAMAP-Rule:MF_00469};
DE EC=1.14.-.- {ECO:0000256|HAMAP-Rule:MF_00469};
DE AltName: Full=tRNA hydroxylation protein O {ECO:0000256|HAMAP-Rule:MF_00469};
GN Name=trhO {ECO:0000256|HAMAP-Rule:MF_00469};
GN ORFNames=HSISM1_1936 {ECO:0000313|EMBL:EQC76608.1};
OS Streptococcus sp. HSISM1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1316408 {ECO:0000313|EMBL:EQC76608.1};
RN [1] {ECO:0000313|EMBL:EQC76608.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSISM1 {ECO:0000313|EMBL:EQC76608.1};
RA Van den Bogert B., Boekhorst J., Herrmann R., Smid E.J., Zoetendal E.G.,
RA Kleerebezem M.;
RT "Comparative Genomics Analysis of Streptococcus Isolates from the Human
RT Small Intestine Reveals their Adaptation to a Highly Dynamic Ecosystem.";
RL PLoS ONE 8:E83418-E83418(2013).
CC -!- FUNCTION: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U)
CC modification at position 34 in tRNAs. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00469};
CC -!- SIMILARITY: Belongs to the TrhO family. {ECO:0000256|HAMAP-
CC Rule:MF_00469}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EQC76608.1}.
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DR EMBL; ASKI01000065; EQC76608.1; -; Genomic_DNA.
DR AlphaFoldDB; T0VAW4; -.
DR PATRIC; fig|1316408.3.peg.1487; -.
DR eggNOG; COG1054; Bacteria.
DR HOGENOM; CLU_038878_1_0_9; -.
DR Proteomes; UP000015933; 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 CDD; cd01518; RHOD_YceA; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 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:SF3; RHODANESE-LIKE DOMAIN-CONTAINING PROTEIN 7-RELATED; 1.
DR PANTHER; PTHR43268; THIOSULFATE SULFURTRANSFERASE/RHODANESE-LIKE DOMAIN-CONTAINING PROTEIN 2; 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; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00469};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00469}.
FT DOMAIN 130..224
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 327 AA; 37796 MW; A91B25EC5DB5CF3C CRC64;
MAKPIRVLLY YKYVPIENAE QFAADHLAFC KSIDLKGRIL VADEGINGTV SGDYETTQKY
MDYVHSLPGM EDLWFKIDEE EEQAFKKMFV RYKKEIVHLG LEDDNFDNDI NPLETTGAYL
SPKEFKEALL DEDTVVLDTR NDYEYDLGHF RGAIRPDIRN FRELPQWVRD NKEKFMDKRV
VVYCTGGVRC EKFSGWMVRE GYKDVGQLHG GIATYGKDPE VQGELWDGKM YVFDERIAVD
VNHVDPSVVG KDWFDGTPCE RYVNCGNPFC NRRILTSEEN EDKYLRGCSH ECRVHPRNRY
VEEHNLSQAE VAERLAVIGE TLDGAPA
//
