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Database: UniProt
Entry: A0A1Q2L1N9_9BACL
LinkDB: A0A1Q2L1N9_9BACL
Original site: A0A1Q2L1N9_9BACL 
ID   A0A1Q2L1N9_9BACL        Unreviewed;       320 AA.
AC   A0A1Q2L1N9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=B0X71_15605 {ECO:0000313|EMBL:AQQ54385.1};
OS   Planococcus lenghuensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX   NCBI_TaxID=2213202 {ECO:0000313|EMBL:AQQ54385.1, ECO:0000313|Proteomes:UP000188184};
RN   [1] {ECO:0000313|EMBL:AQQ54385.1, ECO:0000313|Proteomes:UP000188184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y42 {ECO:0000313|EMBL:AQQ54385.1,
RC   ECO:0000313|Proteomes:UP000188184};
RA   Yang R.;
RT   "The complete genomic sequence of a novel cold adapted crude oil-degrading
RT   bacterium Planococcus qaidamina Y42.";
RL   Submitted (FEB-2017) 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; CP019640; AQQ54385.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2L1N9; -.
DR   KEGG; pmar:B0X71_15605; -.
DR   OrthoDB; 9778326at2; -.
DR   Proteomes; UP000188184; Chromosome.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000188184};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00469}.
FT   DOMAIN          126..220
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   320 AA;  36963 MW;  92DE21802B6DE823 CRC64;
     MQNHTYNVLL FYKYVPIEDP ETFAAEHLEV CKELGLKGRI LVGHEGINGT CSGTIEQTEK
     YTDMLKADPR FSDIVFKIDE TDGHAFKKMH VRFRNEIVNL SLEDDINPNE LTGNYLEPEE
     FYKKMQDENT IVLDARNDYE YDLGHFRGAI RPDIENFRDL PKWVEENREM LEGKEVLTYC
     TGGIRCEKFS GWLKREGFDN VGQLHGGIVT YGKDPEVQGK LWDGQLYVFD ERIAVPVNRV
     EHVIVGRDHF TGEPCERYVN CANPECNKKI LASEENEYKY MRSCSDECRE HPRNRYAAEN
     GLTAAEVQAR LDALKEEASV
//
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