ID A0A261DBC8_9RICK Unreviewed; 254 AA.
AC A0A261DBC8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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 {ECO:0000313|EMBL:OZG31951.1};
GN Synonyms=trhO {ECO:0000256|HAMAP-Rule:MF_00469};
GN ORFNames=RiCNE_06300 {ECO:0000313|EMBL:OZG31951.1};
OS Rickettsia endosymbiont of Culicoides newsteadi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia.
OX NCBI_TaxID=1961830 {ECO:0000313|EMBL:OZG31951.1, ECO:0000313|Proteomes:UP000216097};
RN [1] {ECO:0000313|EMBL:OZG31951.1, ECO:0000313|Proteomes:UP000216097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RiCNE {ECO:0000313|EMBL:OZG31951.1,
RC ECO:0000313|Proteomes:UP000216097};
RX PubMed=28805302;
RA Pilgrim J., Ander M., Garros C., Baylis M., Hurst G.D.D., Siozios S.;
RT "Torix group Rickettsia are widespread in Culicoides biting midges
RT (Diptera: Ceratopogonidae), reach high frequency and carry unique genomic
RT features.";
RL Environ. Microbiol. 19:4238-4255(2017).
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:OZG31951.1}.
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DR EMBL; MWZE01000028; OZG31951.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261DBC8; -.
DR Proteomes; UP000216097; 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:UP000216097};
KW Transferase {ECO:0000313|EMBL:OZG31951.1};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00469}.
FT DOMAIN 129..223
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 254 AA; 28851 MW; 0FE1AB399ED4EC1A CRC64;
MFTMDNNVKI SVLSFYSFTK LENLEVLLPK ILHLGKKRGV RGTILLAPEG FNGSISGAKE
QVNFLLDEII SLTLAEDVNI KINYCDIHPF QKLRIKLKKE IIAMAVGDID IANLKGEYIE
AKDWDKFISQ NNVVVIDTRN DYEVCIGTFK GAIDPKTETF KQFPKWVEQN KDLLVGKKIA
MYCTGGIRCE KSTAYLKKLG FNDVYHLKGG ILQYLEDTHN HSNLWQGECF VFDDRRAVAS
DLSPAEGHWL QRGD
//
