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
//