ID   DUS_STAAC               Reviewed;         328 AA.
AC   Q5HJT5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Probable tRNA-dihydrouridine synthase;
DE            EC=1.3.1.-;
GN   Name=dus; OrderedLocusNames=SACOL0067;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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=AAW38711.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000046; AAW38711.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000662031.1; NC_002951.2.
DR   AlphaFoldDB; Q5HJT5; -.
DR   SMR; Q5HJT5; -.
DR   EnsemblBacteria; AAW38711; AAW38711; SACOL0067.
DR   KEGG; sac:SACOL0067; -.
DR   HOGENOM; CLU_013299_0_3_9; -.
DR   Proteomes; UP000000530; 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; IPR018517; tRNA_hU_synthase_CS.
DR   Pfam; PF01207; Dus; 1.
DR   PIRSF; PIRSF006621; Dus; 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..328
FT                   /note="Probable tRNA-dihydrouridine synthase"
FT                   /id="PRO_0000162142"
FT   ACT_SITE        105
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         143
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         208..210
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         232..233
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
SQ   SEQUENCE   328 AA;  37767 MW;  1A5FBEFF80097E42 CRC64;
     MKENFWSELP RPFFILAPME DVTDIVFRHV VSEAARPDVF FTEFTNTESF CHPEGIHSVR
     GRLTFSEDEQ PMVAHIWGDK PEQFRETSIQ LAKMGFKGID LNMGCPVANV AKKGKGSGLI
     LRPDVAAEII QATKAGGLPV SVKTRLGYYE IDEWKDWLKH VFEQDIANLS IHLRTRKEMS
     KVDAHWELIE AIKNLRDEIA PNTLLTINGD IPDRKTGLEL AEKYGIDGVM IGRGIFHNPF
     AFEKEPREHT SKELLDLLRL HLSLFNKYEK DEIRQFKSLR RFFKIYVRGI RGASELRHQL
     MNTQSIAEAR ALLDEFEAQM DEDVKIEL