DUS_STAAW
ID DUS_STAAW Reviewed; 328 AA.
AC Q8NYV4;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Probable tRNA-dihydrouridine synthase;
DE EC=1.3.1.-;
GN Name=dus; OrderedLocusNames=MW0059;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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; BA000033; BAB93924.1; -; Genomic_DNA.
DR RefSeq; WP_000662031.1; NC_003923.1.
DR AlphaFoldDB; Q8NYV4; -.
DR SMR; Q8NYV4; -.
DR EnsemblBacteria; BAB93924; BAB93924; BAB93924.
DR KEGG; sam:MW0059; -.
DR HOGENOM; CLU_013299_0_3_9; -.
DR OMA; LIYPYVD; -.
DR Proteomes; UP000000418; 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_0000162147"
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