DUSB_SALTI
ID DUSB_SALTI Reviewed; 321 AA.
AC P0A2R7; P37405; Q8Z3D1;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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};
GN OrderedLocusNames=STY3564, t3299;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO70834.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD07899.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL513382; CAD07899.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014613; AAO70834.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_457760.1; NC_003198.1.
DR RefSeq; WP_001219664.1; NZ_WSUR01000038.1.
DR AlphaFoldDB; P0A2R7; -.
DR SMR; P0A2R7; -.
DR STRING; 220341.16504446; -.
DR EnsemblBacteria; AAO70834; AAO70834; t3299.
DR KEGG; stt:t3299; -.
DR KEGG; sty:STY3564; -.
DR PATRIC; fig|220341.7.peg.3629; -.
DR eggNOG; COG0042; Bacteria.
DR HOGENOM; CLU_013299_0_1_6; -.
DR OMA; RPWLFAD; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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; RNA-binding; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..321
FT /note="tRNA-dihydrouridine synthase B"
FT /id="PRO_0000162096"
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"
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
