ID A0A0P1H297_9RHOB Unreviewed; 304 AA.
AC A0A0P1H297;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=TM5383_01644 {ECO:0000313|EMBL:CUH84434.1};
OS Thalassovita mediterranea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassovita.
OX NCBI_TaxID=340021 {ECO:0000313|EMBL:CUH84434.1, ECO:0000313|Proteomes:UP000051681};
RN [1] {ECO:0000313|EMBL:CUH84434.1, ECO:0000313|Proteomes:UP000051681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8383 {ECO:0000313|EMBL:CUH84434.1,
RC ECO:0000313|Proteomes:UP000051681};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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}.
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DR EMBL; CYSF01000007; CUH84434.1; -; Genomic_DNA.
DR RefSeq; WP_058318542.1; NZ_FTNX01000010.1.
DR AlphaFoldDB; A0A0P1H297; -.
DR STRING; 340021.TM5383_01644; -.
DR OrthoDB; 9778326at2; -.
DR Proteomes; UP000051681; 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; 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; 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:UP000051681};
KW Transferase {ECO:0000313|EMBL:CUH84434.1};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00469}.
FT DOMAIN 121..215
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 304 AA; 34034 MW; DF47A363B80583A7 CRC64;
MYIVCALYHF TRFSDPAALK PALLELALEK GVTGSLLLAR EGINGTIAGS RDGIDAVLAH
VRALPGCADL EWKESTAKDA PFPRMKVKLK KEIVTMGQPD VDPLAKVGHY VDPQDWNDLI
RSDDVAVIDT RNDYEVAIGT FEGAVDPETD TFRDFPAWWE ANKERFHNKR IAMFCTGGIR
CEKSTNYLMS QGVEDVYHLK GGILKYLEEV PQEDSSWEGE CFVFDGRVSV GHGLAEGPHV
LCHACRRPIL PEDLKRPEYE DGVTCHLCID EKTEADKARF RERQKQIELA KKRGETHMGG
SRGV
//
