ID D5BN70_PUNMI Unreviewed; 329 AA.
AC D5BN70;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 OrderedLocusNames=SAR116_2020 {ECO:0000313|EMBL:ADE40263.1};
OS Puniceispirillum marinum (strain IMCC1322).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster;
OC Puniceispirillum.
OX NCBI_TaxID=488538 {ECO:0000313|EMBL:ADE40263.1, ECO:0000313|Proteomes:UP000007460};
RN [1] {ECO:0000313|EMBL:ADE40263.1, ECO:0000313|Proteomes:UP000007460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC1322 {ECO:0000313|EMBL:ADE40263.1,
RC ECO:0000313|Proteomes:UP000007460};
RX PubMed=20382761; DOI=10.1128/JB.00347-10;
RA Oh H.M., Kwon K.K., Kang I., Kang S.G., Lee J.H., Kim S.J., Cho J.C.;
RT "Complete genome sequence of "Candidatus Puniceispirillum marinum"
RT IMCC1322, a representative of the SAR116 clade in the
RT Alphaproteobacteria.";
RL J. Bacteriol. 192:3240-3241(2010).
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; CP001751; ADE40263.1; -; Genomic_DNA.
DR AlphaFoldDB; D5BN70; -.
DR KEGG; apb:SAR116_2020; -.
DR eggNOG; COG1054; Bacteria.
DR HOGENOM; CLU_038878_0_0_5; -.
DR Proteomes; UP000007460; 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; 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:UP000007460};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00469}.
FT DOMAIN 141..238
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 307..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 329 AA; 36819 MW; B41BE1306652A4BA CRC64;
MSVMTQNMNE MLLRAEADGR GYVVAAMYKF VTLTDIETLQ QTIINLCTSH QALGTILLAN
EGINGTIAAP IDGMTGILEW LEADSRFGGM SLKFSHSPTQ PFLRMKVRLK REIVTMGCPE
ISPAERTGTY VEPKDWNALI SDPDVLVVDT RNVYETAIGM FDNAVDPMTT NFRDFPDWAA
RLAEQQAPAK PKKIAMYCTG GIRCEKASAL MQDYGFDEVY HLQGGILKYL EDVPKNDSKW
QGECFVFDGR VAVDHNLNPG SYGMCHGCRM PLSQDDMQRP EYVEGISCHH CQDTQDPERT
ARFAERQKQI QLAKHRGEAH LGASPRNSK
//
