DUS_AQUAE
ID DUS_AQUAE Reviewed; 316 AA.
AC O67533;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable tRNA-dihydrouridine synthase;
DE EC=1.3.1.-;
GN Name=dus; OrderedLocusNames=aq_1598;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(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; AE000657; AAC07506.1; -; Genomic_DNA.
DR PIR; C70438; C70438.
DR RefSeq; NP_214098.1; NC_000918.1.
DR RefSeq; WP_010881036.1; NC_000918.1.
DR AlphaFoldDB; O67533; -.
DR SMR; O67533; -.
DR STRING; 224324.aq_1598; -.
DR EnsemblBacteria; AAC07506; AAC07506; aq_1598.
DR KEGG; aae:aq_1598; -.
DR PATRIC; fig|224324.8.peg.1234; -.
DR eggNOG; COG0042; Bacteria.
DR HOGENOM; CLU_013299_0_3_0; -.
DR InParanoid; O67533; -.
DR OMA; RPWLFAD; -.
DR OrthoDB; 1710586at2; -.
DR Proteomes; UP000000798; 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; IPR018517; tRNA_hU_synthase_CS.
DR Pfam; PF01207; Dus; 1.
DR PIRSF; PIRSF006621; Dus; 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..316
FT /note="Probable tRNA-dihydrouridine synthase"
FT /id="PRO_0000162130"
FT ACT_SITE 96
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 12..14
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P33371"
FT BINDING 65
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P33371"
FT BINDING 138
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P33371"
FT BINDING 197..199
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P33371"
FT BINDING 221..222
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P33371"
SQ SEQUENCE 316 AA; 35808 MW; B064E7506A018A90 CRC64;
MNFKKGEVIL APMASYTHSA FRRLCRRLGA DRTYTELISA VGVLRNGIPM KLAYFTEEER
PIHIQVFGSN PEEIAQASVV IAKELKPDFI DINFGCSVPK VLRNKAAGYM LQCPPLMGEV
VKETVEALKP YGIPVSAKIR LGFEKDEVER IVEELQKAGV SLIAIHARTA KQGFSGKALW
HRIKEAKKVA SVPIIGSGDV KSWRDIERMF EETECDGVMV GRAALSNPWI FKEFKEKRDI
EVGLKERMDF ILEELSMMTE YMSREKACAE IKSQIVQILK GVPNSRELKT YIVHAENCKE
LVKRIEEAKE RELLYA