DUSB_SALTY
ID DUSB_SALTY Reviewed; 321 AA.
AC P0A2R6; P37405; Q8Z3D1;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=tRNA-dihydrouridine synthase B {ECO:0000255|HAMAP-Rule:MF_02042};
DE EC=1.3.1.- {ECO:0000255|HAMAP-Rule:MF_02042};
GN Name=dusB {ECO:0000255|HAMAP-Rule:MF_02042}; OrderedLocusNames=STM3384;
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 [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=7536730; DOI=10.1128/jb.177.8.2021-2032.1995;
RA Osuna R., Lienau D., Hughes K.T., Johnson R.C.;
RT "Sequence, regulation, and functions of fis in Salmonella typhimurium.";
RL J. Bacteriol. 177:2021-2032(1995).
RN [2]
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. {ECO:0000255|HAMAP-Rule:MF_02042}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02042};
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02042};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02042};
CC -!- SIMILARITY: Belongs to the Dus family. DusB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02042}.
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DR EMBL; U03101; AAA69019.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22253.1; -; Genomic_DNA.
DR PIR; A56267; A56267.
DR RefSeq; NP_462294.1; NC_003197.2.
DR RefSeq; WP_001219664.1; NC_003197.2.
DR AlphaFoldDB; P0A2R6; -.
DR SMR; P0A2R6; -.
DR STRING; 99287.STM3384; -.
DR PaxDb; P0A2R6; -.
DR EnsemblBacteria; AAL22253; AAL22253; STM3384.
DR GeneID; 1254907; -.
DR KEGG; stm:STM3384; -.
DR PATRIC; fig|99287.12.peg.3585; -.
DR HOGENOM; CLU_013299_0_1_6; -.
DR OMA; RPWLFAD; -.
DR PhylomeDB; P0A2R6; -.
DR BioCyc; SENT99287:STM3384-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:0017150; F:tRNA dihydrouridine synthase activity; IEA:UniProtKB-UniRule.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 1.10.1200.80; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_02042; DusB_subfam; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR InterPro; IPR001269; DUS_fam.
DR InterPro; IPR032887; DusB.
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..321
FT /note="tRNA-dihydrouridine synthase B"
FT /id="PRO_0000162097"
FT ACT_SITE 100
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02042"
FT BINDING 16..18
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02042"
FT BINDING 70
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02042"
FT BINDING 139
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02042"
FT BINDING 200..202
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02042"
FT BINDING 224..225
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02042"
FT CONFLICT 249..252
FT /note="PLPL -> RRAS (in Ref. 1; AAA69019)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="Q -> P (in Ref. 1; AAA69019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 35846 MW; E6F360753D8FB9F6 CRC64;
MRIGQYQLRN RLIAAPMAGI TDRPFRTLCY EMGAGLTVSE MMSSNPQVWE SDKSRLRMVH
VDEPGIRTVQ IAGSDPVEMA DAARINVESG AQIIDINMGC PAKKVNRKLA GSALLQYPDL
VKSILIGVVN AVDVPVTLKI RTGWAPEHRN CVEIAQLAED CGIQALTIHG RTRACLFNGE
AEYDSIRAVK QKVSIPIIAN GDITNPHKAR AVLDYTGADA LMIGRAAQGR PWIFREIQHY
LDTGELLPPL PLAEVKRLLC THVRELHDFY GQAKGYRIAR KHVSWYLQEH APDDQFRRTF
NAIEDASEQL EALEAYFENF A
