ID   DUSA_SALTY              Reviewed;         332 AA.
AC   Q8ZKH4;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=tRNA-dihydrouridine(20/20a) synthase {ECO:0000255|HAMAP-Rule:MF_02041};
DE            EC=1.3.1.- {ECO:0000255|HAMAP-Rule:MF_02041};
DE            EC=1.3.1.91 {ECO:0000255|HAMAP-Rule:MF_02041};
DE   AltName: Full=U20-specific dihydrouridine synthase {ECO:0000255|HAMAP-Rule:MF_02041};
DE            Short=U20-specific Dus {ECO:0000255|HAMAP-Rule:MF_02041};
DE   AltName: Full=tRNA-dihydrouridine synthase A {ECO:0000255|HAMAP-Rule:MF_02041};
GN   Name=dusA {ECO:0000255|HAMAP-Rule:MF_02041}; OrderedLocusNames=STM4243;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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. Specifically modifies U20 and U20a in
CC       tRNAs. {ECO:0000255|HAMAP-Rule:MF_02041}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouridine(20) in tRNA + NADP(+) = H(+) + NADPH +
CC         uridine(20) in tRNA; Xref=Rhea:RHEA:53336, Rhea:RHEA-COMP:13533,
CC         Rhea:RHEA-COMP:13534, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.91;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02041};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouridine(20) in tRNA + NAD(+) = H(+) + NADH +
CC         uridine(20) in tRNA; Xref=Rhea:RHEA:53340, Rhea:RHEA-COMP:13533,
CC         Rhea:RHEA-COMP:13534, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.91;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02041};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouridine(20a) in tRNA + NADP(+) = H(+) + NADPH +
CC         uridine(20a) in tRNA; Xref=Rhea:RHEA:53344, Rhea:RHEA-COMP:13535,
CC         Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02041};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouridine(20a) in tRNA + NAD(+) = H(+) + NADH +
CC         uridine(20a) in tRNA; Xref=Rhea:RHEA:53348, Rhea:RHEA-COMP:13535,
CC         Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02041};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02041};
CC   -!- SIMILARITY: Belongs to the Dus family. DusA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02041}.
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DR   EMBL; AE006468; AAL23067.1; -; Genomic_DNA.
DR   RefSeq; NP_463108.1; NC_003197.2.
DR   RefSeq; WP_001182237.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZKH4; -.
DR   SMR; Q8ZKH4; -.
DR   STRING; 99287.STM4243; -.
DR   PaxDb; Q8ZKH4; -.
DR   EnsemblBacteria; AAL23067; AAL23067; STM4243.
DR   GeneID; 1255769; -.
DR   KEGG; stm:STM4243; -.
DR   PATRIC; fig|99287.12.peg.4463; -.
DR   HOGENOM; CLU_013299_2_1_6; -.
DR   OMA; LIYPYVD; -.
DR   PhylomeDB; Q8ZKH4; -.
DR   BioCyc; SENT99287:STM4243-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0102264; F:tRNA-dihydrouridine20 synthase activity; IEA:UniProtKB-EC.
DR   CDD; cd02801; DUS_like_FMN; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_02041; DusA_subfam; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035587; DUS-like_FMN-bd.
DR   InterPro; IPR001269; DUS_fam.
DR   InterPro; IPR004653; DusA.
DR   InterPro; IPR018517; tRNA_hU_synthase_CS.
DR   PANTHER; PTHR42907; PTHR42907; 1.
DR   Pfam; PF01207; Dus; 1.
DR   PIRSF; PIRSF006621; Dus; 1.
DR   TIGRFAMs; TIGR00742; yjbN; 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..332
FT                   /note="tRNA-dihydrouridine(20/20a) synthase"
FT                   /id="PRO_0000162073"
FT   ACT_SITE        101
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT   BINDING         19..21
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT   BINDING         71
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT   BINDING         140
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT   BINDING         173
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT   BINDING         213..215
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT   BINDING         235..236
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT   SITE            98
FT                   /note="Interacts with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT   SITE            185
FT                   /note="Interacts with tRNA; defines subfamily-specific
FT                   binding signature"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT   SITE            188
FT                   /note="Interacts with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT   SITE            301
FT                   /note="Interacts with tRNA; defines subfamily-specific
FT                   binding signature"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT   SITE            304
FT                   /note="Interacts with tRNA; defines subfamily-specific
FT                   binding signature"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
SQ   SEQUENCE   332 AA;  36986 MW;  B2E14334AA2ADD7E CRC64;
     MQPETQSSAL PAYRFSIAPM LDWTDRHCRY FLRLLSRQTQ LYTEMVTTGA IIHGKGDYLA
     YSEEEHPVAL QLGGSDPAQL AHCAKLAEAR GYDEINLNVG CPSDRVQNGM FGACLMGNAQ
     LVADCVKAMR DVVSIPVTVK TRIGIDDQDS YAFLCDFIDT VSGQGECEMF IIHARKAWLS
     GLSPKENREI PPLDYPRVYQ LKRDFPHLTM SINGGIKSLE EAKEHLRHMD GVMVGREAYQ
     NPGILAAVDR EIFGADTTDA DPVAVVRAMY PYIERELSQG AYLGHITRHM LGLFQGIPGA
     RQWRRYLSEN AHKAGADVAV LEQALKLVAD KR