ID   DUS_RHILP               Reviewed;         317 AA.
AC   P41504;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Probable tRNA-dihydrouridine synthase;
DE            EC=1.3.1.-;
GN   Name=dus;
OS   Rhizobium leguminosarum bv. phaseoli.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CE-3;
RX   PubMed=8412703; DOI=10.1111/j.1365-2958.1993.tb01717.x;
RA   Patriarca E.J., Riccio A., Tate R., Colonna-Romano S., Iaccarino M.,
RA   Defez R.;
RT   "The ntrBC genes of Rhizobium leguminosarum are part of a complex operon
RT   subject to negative regulation.";
RL   Mol. Microbiol. 9:569-577(1993).
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}.
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DR   EMBL; X71436; CAA50567.1; -; Genomic_DNA.
DR   PIR; S36201; S36201.
DR   AlphaFoldDB; P41504; -.
DR   SMR; P41504; -.
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; RNA-binding; tRNA processing;
KW   tRNA-binding.
FT   CHAIN           1..317
FT                   /note="Probable tRNA-dihydrouridine synthase"
FT                   /id="PRO_0000162138"
FT   ACT_SITE        94
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT   BINDING         11..13
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         64
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         133
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         194..196
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         218..219
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
SQ   SEQUENCE   317 AA;  34604 MW;  57E3F79FC9B18B48 CRC64;
     MSVRNRVVLA PMSGVTDMPF RELAWRFGAG LVVTEMVASR ELVNDTAESW SRLKAAGFRP
     HMVQLAGREA HWMAEAAKIA ADHGADIIDI NMGCPAKKVI GGYSGSALMR DPDHALGLIE
     ATVKAVDIPV TLKMRLGWDE NSINAPDIAR RAEASGIQLV TIHGRTRMQF YEGRADWDAI
     RAVREVISVP LIANGDVETA HDAQEILRRS GADAVMIGRG CQGRPWHAGV LAGAAEPRRE
     DIADIAVEHY RMMLDFYGEA VAIRHARKHL GWYLERFAPA LAGTEKAGIM TSRDPREVAA
     RLYHALDAGA LDGREAA