ID A0A0N0D7S2_9RHOB Unreviewed; 302 AA.
AC A0A0N0D7S2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=glpE_3 {ECO:0000313|EMBL:KPA19984.1};
GN Synonyms=trhO {ECO:0000256|HAMAP-Rule:MF_00469};
GN ORFNames=shim_39430 {ECO:0000313|EMBL:KPA19984.1};
OS Shimia sp. SK013.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1389006 {ECO:0000313|EMBL:KPA19984.1, ECO:0000313|Proteomes:UP000037951};
RN [1] {ECO:0000313|EMBL:KPA19984.1, ECO:0000313|Proteomes:UP000037951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK013 {ECO:0000313|EMBL:KPA19984.1,
RC ECO:0000313|Proteomes:UP000037951};
RA Voget S., Kanukollu S., Daniel R., Engelen B.;
RT "Genome Sequence of Shimia sp. SK013.";
RL Submitted (MAR-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}.
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:KPA19984.1}.
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DR EMBL; LAJH01000028; KPA19984.1; -; Genomic_DNA.
DR RefSeq; WP_054004349.1; NZ_LAJH01000028.1.
DR AlphaFoldDB; A0A0N0D7S2; -.
DR STRING; 1389006.shim_39430; -.
DR PATRIC; fig|1389006.3.peg.4071; -.
DR OrthoDB; 9778326at2; -.
DR Proteomes; UP000037951; 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:UP000037951};
KW Transferase {ECO:0000313|EMBL:KPA19984.1};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00469}.
FT DOMAIN 121..215
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 302 AA; 34105 MW; E196D1B1CA022367 CRC64;
MFTVCALYHF SRFENHEALR PPLLELCLKE GITGTLLLAP EGINGTIAGT RKGIDAIIAH
IQSLPGCANF EWKLSTASDK PFPRMKVKLK KEIVTLGQPN VDPTAHVGNY VTPQDWNELI
QSPDVVTIDT RNDYEVAIGT FQGAVDPETA SFREFPAWWE ENKDRFHNKR VAMFCTGGIR
CEKSTNFLMS QGVEEVYHLK GGILKYLEEV PQEDSTWDGE CFVFDGRVSV GHALKEGPHV
LCHACRRPIL PEDLARPEYE AGVSCHHCVD ESSERDKARF RERQKQMLLA RERGEQHIIG
LD
//
