ID A0A370EGD7_9FLAO Unreviewed; 450 AA.
AC A0A370EGD7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=DEU42_1128 {ECO:0000313|EMBL:RDI07918.1};
OS Flavobacterium sp. AG291.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2184000 {ECO:0000313|EMBL:RDI07918.1, ECO:0000313|Proteomes:UP000254305};
RN [1] {ECO:0000313|EMBL:RDI07918.1, ECO:0000313|Proteomes:UP000254305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG291 {ECO:0000313|EMBL:RDI07918.1,
RC ECO:0000313|Proteomes:UP000254305};
RA Venturi V.;
RT "Genome sequencing of rice bacterial endophytes.";
RL Submitted (JUL-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:RDI07918.1}.
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DR EMBL; QQAR01000012; RDI07918.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370EGD7; -.
DR OrthoDB; 9778326at2; -.
DR Proteomes; UP000254305; 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: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; PTHR43846:SF1; TRNA URIDINE(34) HYDROXYLASE; 1.
DR PANTHER; PTHR43846; UPF0176 PROTEIN YCEA; 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 Reference proteome {ECO:0000313|Proteomes:UP000254305};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00469}.
FT DOMAIN 144..239
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 450 AA; 50625 MW; C088AF106E81D1B4 CRC64;
MQLFNTLSAE ERTALIEESG KQRLTLSFYA YAHISDPKQF RDSLFLAWNP LEVLGRIYVA
KEGINAQLSL PADHFYEFKD HLDTIPFLKD IRLNVAVEQD DLSFLKLTIK VRDKVVADGL
NDDTFDVTNI GVHLKAQEFN DMLEHPDTIV VDMRNHYESE IGHFRGAITP DVDTFRESLP
IIEEQLSEYK EGKNLLMYCT GGIRCEKASA FFKHKGFQNV YQLEGGIIEY TRQVKAEGLE
SKFIGKNFVF DARLGERITD DIVSQCHQCG KPCDNHTNCA NEACHLLFIQ CDECKDASQN
CCSEACQDVV NLPVEEQKAL RRGIMNGNMI FKKGKADRLT FKKTGTEVSD VALGTAAKTK
TVRPRIRKTL VGKGEHYFPK AEVAQFIMES ELAVGDTVII SGPTTGEQQL VIEKMRVNGQ
DGTTAAKGDK VTFSVPFRIR LSDKLFKVIG
//
