ID A0A0Q0G8M0_9GAMM Unreviewed; 325 AA.
AC A0A0Q0G8M0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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_1 {ECO:0000313|EMBL:KPZ70853.1};
GN Synonyms=trhO {ECO:0000256|HAMAP-Rule:MF_00469};
GN ORFNames=AN944_01951 {ECO:0000313|EMBL:KPZ70853.1};
OS Shewanella sp. P1-14-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=1723761 {ECO:0000313|EMBL:KPZ70853.1, ECO:0000313|Proteomes:UP000050414};
RN [1] {ECO:0000313|EMBL:KPZ70853.1, ECO:0000313|Proteomes:UP000050414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-14-1 {ECO:0000313|EMBL:KPZ70853.1,
RC ECO:0000313|Proteomes:UP000050414};
RA Gilbert D.G.;
RL Submitted (OCT-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:KPZ70853.1}.
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DR EMBL; LKTL01000011; KPZ70853.1; -; Genomic_DNA.
DR RefSeq; WP_055024397.1; NZ_LKTL01000011.1.
DR AlphaFoldDB; A0A0Q0G8M0; -.
DR PATRIC; fig|1723761.3.peg.1996; -.
DR Proteomes; UP000050414; 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:UP000050414};
KW Transferase {ECO:0000313|EMBL:KPZ70853.1};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00469}.
FT DOMAIN 123..217
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 325 AA; 37174 MW; B6808BA52FC82AAD CRC64;
MSQVVVCALY KFVALPHYEA IRAPLLDKME SSEIRGTLLL AKEGINGTVA GSQQAIDGLL
EWLATQDGLA DIVYKLSFDD NMPFYRTKVK LKKEIVTMGV EGIDPREVVG TYVKPKDWNQ
LISDPEVLLV DTRNDYEVQI GTFKNAVNPV TETFREFPEY VKENLDPNKH KKVAMFCTGG
IRCEKSTAYL KEQGFDEVYH LEGGILKYLE EVKPEQSLWE GECFVFDNRV AVNHQLEKGV
YDQCNACRMP ITQEEMQTEA YVQGVSCPHC IDKISDEQRQ RFIERERQVQ LAKQRGEAHI
GSEVKQVIAQ RRKQKETQKQ AQNES
//
