ID   DUS_RHOCB               Reviewed;         324 AA.
AC   Q08111; D5AUA2;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Probable tRNA-dihydrouridine synthase;
DE            EC=1.3.1.-;
DE   AltName: Full=Nitrogen regulation protein nifR3;
GN   Name=dus; Synonyms=dusB, nifR3; OrderedLocusNames=RCAP_rcc01796;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=8355615; DOI=10.1111/j.1365-2958.1993.tb01636.x;
RA   Foster-Hartnett D., Cullen P.J., Gabbert K.K., Kranz R.G.;
RT   "Sequence, genetic, and lacZ fusion analyses of a nifR3-ntrB-ntrC operon in
RT   Rhodobacter capsulatus.";
RL   Mol. Microbiol. 8:903-914(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
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   -!- CAUTION: Was originally thought to be involved in the activation of
CC       nitrogen assimilatory genes. {ECO:0000305|PubMed:8355615}.
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DR   EMBL; X72382; CAA51073.1; -; Genomic_DNA.
DR   EMBL; CP001312; ADE85541.1; -; Genomic_DNA.
DR   PIR; S34981; S34981.
DR   RefSeq; WP_013067520.1; NC_014034.1.
DR   AlphaFoldDB; Q08111; -.
DR   SMR; Q08111; -.
DR   STRING; 272942.RCAP_rcc01796; -.
DR   EnsemblBacteria; ADE85541; ADE85541; RCAP_rcc01796.
DR   GeneID; 31490671; -.
DR   KEGG; rcp:RCAP_rcc01796; -.
DR   eggNOG; COG0042; Bacteria.
DR   HOGENOM; CLU_013299_0_1_5; -.
DR   OMA; RPWLFAD; -.
DR   OrthoDB; 1710586at2; -.
DR   Proteomes; UP000002361; 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..324
FT                   /note="Probable tRNA-dihydrouridine synthase"
FT                   /id="PRO_0000162139"
FT   ACT_SITE        103
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT   BINDING         18..20
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         73
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         142
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         203..205
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         227..228
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
SQ   SEQUENCE   324 AA;  33939 MW;  F456044CEBF34207 CRC64;
     MTISLDSLRL DPPVLLAPMA GITDLPFRRM VARFGAGLVV SEMVASGEML TAKPSVRAKA
     QAELTAGLPT SVQLAGREAA PMAEAAKIVA DMGAEIIDIN MGCPAKKVTG GLSGAALMRN
     PDHALRLIEA VVGAVDLPVT LKMRLGWDED QLNAAEIAAR AEAAGVKMIV IHGRTRMQFY
     TGAADWRAIA AVRAAVSVPV VANGDITDAA SARRALDQSG AAGVMVGRGA QGAPWRLAQI
     AAALFGKADP KLPSGSEFSD FVSEHYEAIL SFYGRDLGLR IARKHLGWYA EAAAAPLRAE
     MMRATDPAAT LALIRSAFSE REAA