ID T0IVN2_9SPHN Unreviewed; 341 AA.
AC T0IVN2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=L284_13830 {ECO:0000313|EMBL:EQB13749.1};
OS Novosphingobium lindaniclasticum LE124.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1096930 {ECO:0000313|EMBL:EQB13749.1, ECO:0000313|Proteomes:UP000015527};
RN [1] {ECO:0000313|EMBL:EQB13749.1, ECO:0000313|Proteomes:UP000015527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LE124 {ECO:0000313|EMBL:EQB13749.1,
RC ECO:0000313|Proteomes:UP000015527};
RX PubMed=24029761;
RA Saxena A., Nayyar N., Sangwan N., Kumari R., Khurana J.P., Lal R.;
RT "Genome Sequence of Novosphingobium lindaniclasticum LE124T, Isolated from
RT a Hexachlorocyclohexane Dumpsite.";
RL Genome Announc. 1:e00715-13(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:EQB13749.1}.
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DR EMBL; ATHL01000086; EQB13749.1; -; Genomic_DNA.
DR AlphaFoldDB; T0IVN2; -.
DR PATRIC; fig|1096930.3.peg.2752; -.
DR eggNOG; COG1054; Bacteria.
DR Proteomes; UP000015527; 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; 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:UP000015527};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00469}.
FT DOMAIN 143..245
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 300..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 341 AA; 37236 MW; 7198EBA59F474AFC CRC64;
MQNGCAQMND SGDLSGRVPV SEPVCVAALY QFTRFVDAAA LRAPLLALCE EQGIKGTLLL
AAEGINGTIA GSHEGIEQVL SHVRALPGCA EVDVKLSGAQ TMPFHRMKVR LKCEIVTMGQ
PDIDPLSVVG TYVEPQDWNA LISDPDTIVI DTRNDYEVAV GTFSGAVDPR TATFRDFPAW
FRAERDKLLA AKGEGGRPPK VAMFCTGGIR CEKSTAFLKQ EGVDEVFHLK GGILKYLETV
PEEESLWRGE CFVFDQRVTI GHGLVQGSHA LCHACRRPVN AQDRTSPLYE EGVSCPACHQ
ERSDEQRASY RERHRQEALA AERGELHVGA VRKAETETDA G
//