DUSB_SHIFL
ID DUSB_SHIFL Reviewed; 321 AA.
AC Q83PZ5; Q7UBE2;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=SF3298, S3515;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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=AAN44762.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP18573.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN44762.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP18573.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_709055.2; NC_004337.2.
DR RefSeq; WP_001219649.1; NZ_WPGW01000026.1.
DR AlphaFoldDB; Q83PZ5; -.
DR SMR; Q83PZ5; -.
DR STRING; 198214.SF3298; -.
DR EnsemblBacteria; AAN44762; AAN44762; SF3298.
DR EnsemblBacteria; AAP18573; AAP18573; S3515.
DR GeneID; 1023434; -.
DR GeneID; 58389329; -.
DR KEGG; sfl:SF3298; -.
DR KEGG; sfx:S3515; -.
DR PATRIC; fig|198214.7.peg.3906; -.
DR HOGENOM; CLU_013299_0_1_6; -.
DR OrthoDB; 1710586at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000162100"
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; 35822 MW; E9A318C459825C4E CRC64;
MRIGQYQLRN RLIAAPMAGI TDRPFRTLCY EMGAGLTVSE MMSSNPQVWE SDKSRLRMVH
IDEPGIRTVQ IAGSAPKEMA DAARINVESG AQIIDINMGC PAKKVNRKLA GSALLQYPDV
VKSILTEVVN AVDVPVTLKI RTGWAPEHRN CEEIAQLAED CGIQALTIHG RTRACLFNGE
AEYDSIRAVK QKVSIPVIAN GDITDPLKAR AVLDYTGADA LMIGRAAQGR PWIFREIQHY
LDTGELLPPL PLAEVKRLLC AHVRELHDFY GPAKGYRIAR KHVSWYLQEH APNDQFRRTF
NAIEDASEQL EALEAYFENF A
