ID   DUSB_PECCA              Reviewed;         321 AA.
AC   O52539;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1999, sequence version 2.
DT   03-AUG-2022, entry version 81.
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};
OS   Pectobacterium carotovorum (Erwinia carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9811652; DOI=10.1128/jb.180.22.5932-5946.1998;
RA   Beach M.B., Osuna R.;
RT   "Identification and characterization of the fis operon in enteric
RT   bacteria.";
RL   J. Bacteriol. 180:5932-5946(1998).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF040381; AAC77892.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52539; -.
DR   SMR; O52539; -.
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_0000162087"
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;  35655 MW;  7543831E1F4B5CAD CRC64;
     MHIGQFQLTN RLIAAPMAGI SDRPFRALCH AMGAGMTVSE MLSSNPEVWR SDKSRLRMVH
     SDEPGIRAVQ IAGCDPDEMA AARRINADSG AQIIDINMGC PAKKVNRKMA GSALLQYPDL
     VKQILSTVVK AVDVPVTLKI RTGWAPEHRN CVEIAKLAED CGIQALTIHG RTRACLFNGF
     AEYDSIRAVK QAVSIPIIAN GDITDPHKAR AVLDYTGADA LMIGRAAQGR PWIFREIQHY
     LDTGELLAPL PLVEVKRLLI EHIRELHDFY GPGKGFRIAR KHVSWYLQEH APNDQFRRTF
     NAIEDASEQL EALKAYFENL A