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Database: UniProt
Entry: T0IVN2_9SPHN
LinkDB: T0IVN2_9SPHN
Original site: T0IVN2_9SPHN 
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
//
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