ID   DUSB_VIBCH              Reviewed;         322 AA.
AC   Q9KV66;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 2.
DT   03-AUG-2022, entry version 108.
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=VC_0291;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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=AAF93465.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE003852; AAF93465.1; ALT_INIT; Genomic_DNA.
DR   PIR; B82341; B82341.
DR   RefSeq; NP_229946.1; NC_002505.1.
DR   RefSeq; WP_001905559.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KV66; -.
DR   SMR; Q9KV66; -.
DR   STRING; 243277.VC_0291; -.
DR   DNASU; 2615014; -.
DR   EnsemblBacteria; AAF93465; AAF93465; VC_0291.
DR   KEGG; vch:VC_0291; -.
DR   PATRIC; fig|243277.26.peg.273; -.
DR   eggNOG; COG0042; Bacteria.
DR   HOGENOM; CLU_013299_0_1_6; -.
DR   OMA; RPWLFAD; -.
DR   Proteomes; UP000000584; Chromosome 1.
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..322
FT                   /note="tRNA-dihydrouridine synthase B"
FT                   /id="PRO_0000162101"
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   322 AA;  35499 MW;  7A8C284584340FE9 CRC64;
     MKIGNYQLKN NLIVAPMAGV TDRPFRELCL RYGAGMAVSE MMSCNPALWK TAKSQNRMVH
     EGESGIRSVQ IAGSDPQLMA EAAQFSVENG AQIIDINMGC PAKKVNKKLA GSALLRYPDV
     IEDILKAVVN AVNVPVTLKT RTGWDTDNKN CLSIAQLAED CGIQALALHG RTRACMYKGE
     AEYDSIKAVK AAVSIPVIAN GDIDSPEKAR YVLEYTGADA LMIGRPAQGR PWIFQEIQHF
     LEHGTTMPEL PISEVKDIML GHVTALHQFY GEYLGPRIAR KHVSWYLQEH EQASAFRRTF
     NAIETADQQL DALEGYFDNV AS