ID   DUSC_AZOVI              Reviewed;         309 AA.
AC   P96192;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=tRNA-dihydrouridine(16) synthase {ECO:0000255|HAMAP-Rule:MF_02043};
DE            EC=1.3.1.- {ECO:0000255|HAMAP-Rule:MF_02043};
DE   AltName: Full=U16-specific dihydrouridine synthase {ECO:0000255|HAMAP-Rule:MF_02043};
DE            Short=U16-specific Dus {ECO:0000255|HAMAP-Rule:MF_02043};
DE   AltName: Full=tRNA-dihydrouridine synthase C {ECO:0000255|HAMAP-Rule:MF_02043};
GN   Name=dusC {ECO:0000255|HAMAP-Rule:MF_02043};
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX   PubMed=9108283; DOI=10.1007/s004380050409;
RA   Manna A.C., Das H.K.;
RT   "Characterization and mutagenesis of the leucine biosynthetic genes of
RT   Azotobacter vinelandii: an analysis of the rarity of amino acid
RT   auxotrophs.";
RL   Mol. Gen. Genet. 254:207-217(1997).
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. Specifically modifies U16 in tRNAs.
CC       {ECO:0000255|HAMAP-Rule:MF_02043}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouridine(16) in tRNA + NADP(+) = H(+) + NADPH +
CC         uridine(16) in tRNA; Xref=Rhea:RHEA:53376, Rhea:RHEA-COMP:13543,
CC         Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02043};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouridine(16) in tRNA + NAD(+) = H(+) + NADH +
CC         uridine(16) in tRNA; Xref=Rhea:RHEA:53380, Rhea:RHEA-COMP:13543,
CC         Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02043};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02043};
CC   -!- SIMILARITY: Belongs to the Dus family. DusC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02043}.
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DR   EMBL; Y11280; CAA72146.1; -; Genomic_DNA.
DR   AlphaFoldDB; P96192; -.
DR   SMR; P96192; -.
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; 3.20.20.70; -; 2.
DR   HAMAP; MF_02043; DusC_subfam; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035587; DUS-like_FMN-bd.
DR   InterPro; IPR032886; DusC.
DR   InterPro; IPR018517; tRNA_hU_synthase_CS.
DR   PANTHER; PTHR11082:SF26; PTHR11082:SF26; 2.
DR   Pfam; PF01207; Dus; 2.
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..309
FT                   /note="tRNA-dihydrouridine(16) synthase"
FT                   /id="PRO_0000162108"
FT   ACT_SITE        98
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT   BINDING         7..9
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT   BINDING         68
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT   BINDING         137
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         198
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         220..221
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT   SITE            35
FT                   /note="Interacts with tRNA; defines subfamily-specific
FT                   binding signature"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT   SITE            95
FT                   /note="Interacts with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT   SITE            175
FT                   /note="Interacts with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02043"
FT   SITE            267
FT                   /note="Interacts with tRNA; defines subfamily-specific
FT                   binding signature"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   SITE            286
FT                   /note="Interacts with tRNA; defines subfamily-specific
FT                   binding signature"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
SQ   SEQUENCE   309 AA;  33181 MW;  2D40B965C6DF551B CRC64;
     MRIALAPMEG LVDELLRDLL TRVGGIDWCV TEFVRVCDRL LPVAQFEKLA PELRHGWRTR
     AGTPMHLQLL GSDPACLAEN AALAAELGAP AIDLNFGCPA KTSTARGADG CCSTSRNCCM
     PSSARCAGPC RRCAGDRQDA PGVRPARGRP GVRRALVEGG VAHLVVHART KVEGYRPPAS
     WEWLARVREA VAVPVYANRK SGRRRIGCRE ISGVEDVMLG CGLVSRPDLA RQIAMRAPDA
     RSSRRAGVRY SRWCASSGGA PGSGSRRATP LAGSSSGWAC WRAVIRRRPR CSPNCAGRTT
     AGGWMPCWA