ID   DUS_RICPR               Reviewed;         327 AA.
AC   Q9ZED2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Probable tRNA-dihydrouridine synthase;
DE            EC=1.3.1.-;
GN   Name=dus; OrderedLocusNames=RP011;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
CC   -!- FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified
CC       base found in the D-loop of most tRNAs, via the reduction of the C5-C6
CC       double bond in target uridines. {ECO:0000250|UniProtKB:P33371}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA +
CC         H(+) + NADH; Xref=Rhea:RHEA:54452, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC         COMP:13887, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC         Evidence={ECO:0000250|UniProtKB:P33371};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5,6-dihydrouridine in tRNA + NADP(+) = a uridine in tRNA +
CC         H(+) + NADPH; Xref=Rhea:RHEA:23624, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC         COMP:13887, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC         Evidence={ECO:0000250|UniProtKB:P33371};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P33371};
CC   -!- SIMILARITY: Belongs to the Dus family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA14483.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ235270; CAA14483.1; ALT_INIT; Genomic_DNA.
DR   PIR; D71708; D71708.
DR   RefSeq; NP_220406.1; NC_000963.1.
DR   RefSeq; WP_014411626.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZED2; -.
DR   SMR; Q9ZED2; -.
DR   STRING; 272947.RP011; -.
DR   EnsemblBacteria; CAA14483; CAA14483; CAA14483.
DR   GeneID; 57569139; -.
DR   KEGG; rpr:RP011; -.
DR   PATRIC; fig|272947.5.peg.11; -.
DR   eggNOG; COG0042; Bacteria.
DR   HOGENOM; CLU_013299_0_3_5; -.
DR   Proteomes; UP000002480; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:InterPro.
DR   CDD; cd02801; DUS_like_FMN; 1.
DR   Gene3D; 1.10.1200.80; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035587; DUS-like_FMN-bd.
DR   InterPro; IPR001269; DUS_fam.
DR   InterPro; IPR024036; tRNA-dHydroUridine_Synthase_C.
DR   InterPro; IPR004652; tRNA_dU_NifR3.
DR   InterPro; IPR018517; tRNA_hU_synthase_CS.
DR   Pfam; PF01207; Dus; 1.
DR   PIRSF; PIRSF006621; Dus; 1.
DR   TIGRFAMs; TIGR00737; nifR3_yhdG; 1.
DR   PROSITE; PS01136; UPF0034; 1.
PE   3: Inferred from homology;
KW   Flavoprotein; FMN; NADP; Oxidoreductase; Reference proteome; RNA-binding;
KW   tRNA processing; tRNA-binding.
FT   CHAIN           1..327
FT                   /note="Probable tRNA-dihydrouridine synthase"
FT                   /id="PRO_0000162141"
FT   ACT_SITE        102
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT   BINDING         17..19
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         72
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         141
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         202..204
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         226..227
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
SQ   SEQUENCE   327 AA;  35789 MW;  AAE4B4D4A87555CC CRC64;
     MIKIGNIELS SNVILAPMSD VTDLEFRKLV KRFGAGLVVS EMIASRAMIM KSRQSMQKCA
     IMHDDPTSAC VQLAGCEPDV IAEAAKMNED MGAKIIDLNF GCPAKKVVGG YAGSALMRDE
     QLAAKIFEAT VKAVKIPVTV KMRIGWDDNT RNAPTLAKIA ANSGVQMVTV HGRTRCQFYS
     GNANWDFIRT VKEAVKIPVI ANGDITNFAK AKEALQRSGA DGIMVGRGVY GKPWLISQIA
     YYLKTGKEKP APSIAEQLDI ITKHYDAIID YYGKSVGVPI ARKHIIWYSN GLPSSAEFRC
     TVNLMKDPIA VKEKIAEFYM SVMDANK