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Database: UniProt
Entry: A0A399RQS0_9BACT
LinkDB: A0A399RQS0_9BACT
Original site: A0A399RQS0_9BACT 
ID   A0A399RQS0_9BACT        Unreviewed;       322 AA.
AC   A0A399RQS0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=D1627_17855 {ECO:0000313|EMBL:RIJ33478.1};
OS   Pontibacter oryzae.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=2304593 {ECO:0000313|EMBL:RIJ33478.1, ECO:0000313|Proteomes:UP000266005};
RN   [1] {ECO:0000313|Proteomes:UP000266005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIRAN {ECO:0000313|Proteomes:UP000266005};
RA   Seo T.;
RT   "Mucilaginibacter sp. MYSH2.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:RIJ33478.1}.
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DR   EMBL; QWGE01000007; RIJ33478.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A399RQS0; -.
DR   OrthoDB; 9778326at2; -.
DR   Proteomes; UP000266005; Unassembled WGS sequence.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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|HAMAP-Rule:MF_00469};
KW   Transferase {ECO:0000313|EMBL:RIJ33478.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00469}.
FT   DOMAIN          124..218
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   322 AA;  36630 MW;  92D2D9111C5E091D CRC64;
     MNKPYSILLY YCYAPIEDPE AYREQHHLLC LELNLLGRII VSKEGLNGTV SGLKEDCEKY
     MAIMHADPRF AKTDFKVDAS DAHAFTKLHV RTKAEIVHSG LLHIDPNKRT GKHLEPKEFK
     AMKDRDDVVV LDVRSDYEHS VGRFKNAVTL DIENFREFPE KVNELKEKYK DKKILTYCTG
     GIKCEKASAF LLEEGFENVY QLHGGIIKYG MEAGGEDFEG KCYVFDNRVA VDVNSVNPTI
     VSECHVCKTK SDRMVNCANP VCNLHVPICE ACGWELEGAC SAECKEHPEK RPYDGTGYYQ
     KELNGYNPLK GFNRKKKTDV QV
//
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