ID   DUS_TREPA               Reviewed;         340 AA.
AC   O83945;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Probable tRNA-dihydrouridine synthase;
DE            EC=1.3.1.-;
GN   Name=dus; OrderedLocusNames=TP_0980;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(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:0000250|UniProtKB:P33371}.
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;
CC         Evidence={ECO:0000250|UniProtKB:P33371};
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;
CC         Evidence={ECO:0000250|UniProtKB:P33371};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P33371};
CC   -!- SIMILARITY: Belongs to the Dus family. {ECO:0000305}.
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DR   EMBL; AE000520; AAC65935.1; -; Genomic_DNA.
DR   PIR; B71258; B71258.
DR   RefSeq; WP_010882424.1; NC_021490.2.
DR   AlphaFoldDB; O83945; -.
DR   SMR; O83945; -.
DR   STRING; 243276.TPANIC_0980; -.
DR   EnsemblBacteria; AAC65935; AAC65935; TP_0980.
DR   GeneID; 57879489; -.
DR   KEGG; tpa:TP_0980; -.
DR   eggNOG; COG0042; Bacteria.
DR   eggNOG; COG3116; Bacteria.
DR   HOGENOM; CLU_013299_0_3_12; -.
DR   OMA; RPWLFAD; -.
DR   OrthoDB; 1710586at2; -.
DR   Proteomes; UP000000811; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:InterPro.
DR   CDD; cd02801; DUS_like_FMN; 1.
DR   Gene3D; 1.10.1200.80; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035587; DUS-like_FMN-bd.
DR   InterPro; IPR001269; DUS_fam.
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..340
FT                   /note="Probable tRNA-dihydrouridine synthase"
FT                   /id="PRO_0000162152"
FT   ACT_SITE        110
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT   BINDING         25..27
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         79
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         154
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         219..221
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         243..244
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
SQ   SEQUENCE   340 AA;  37161 MW;  DA20D42AA88AA71C CRC64;
     MQQHALYHPV SIGPLSLKGN VFFAPVAGYS DSAFRSIAIE WEASFTYTEM VSSEAMVRDS
     LNTKRLIRRA SNETHYAIQI FGSNPAVMAE TAKLIVDSAQ PSCIDINAGC PMPKITKTGA
     GAALTREPTR LYEVVKAVAD AVYAQDARIP VTVKIRAGWE EAHLTWKEAA RAAVDAGAQA
     LALHPRTCAQ CYAGEANWDI IADLVQCARG WGEVPVFGSG DLHAPEDARA MLEHTACAGV
     MFARGAMGNP FIFRQTRQLL TEGYYTPVTF EQKLRAAWRE LHLLAQDVGE SSACKQMRKR
     FVSYAKGERG KTQWCQRAVH ASSFADFAAV IRDACPCIGL