ID DUS3_PICST Reviewed; 613 AA. AC A3LUK5; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 1. DT 03-MAY-2023, entry version 94. DE RecName: Full=tRNA-dihydrouridine(47) synthase [NAD(P)(+)]; DE EC=1.3.1.89 {ECO:0000250|UniProtKB:Q06053}; DE AltName: Full=mRNA-dihydrouridine synthase DUS3; DE EC=1.3.1.- {ECO:0000250|UniProtKB:Q9UTH9}; DE AltName: Full=tRNA-dihydrouridine synthase 3; GN Name=DUS3; ORFNames=PICST_83606; OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL OS Y-11545) (Yeast) (Pichia stipitis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces. OX NCBI_TaxID=322104; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545; RX PubMed=17334359; DOI=10.1038/nbt1290; RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., RA Passoth V., Richardson P.M.; RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting RT yeast Pichia stipitis."; RL Nat. Biotechnol. 25:319-326(2007). CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base CC found in the D-loop of most tRNAs. Specifically modifies U47 in CC cytoplasmic tRNAs (By similarity). Catalyzes the synthesis of CC dihydrouridine in some mRNAs, thereby affecting their translation (By CC similarity). {ECO:0000250|UniProtKB:Q06053, CC ECO:0000250|UniProtKB:Q9UTH9}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5,6-dihydrouridine(47) in tRNA + NAD(+) = H(+) + NADH + CC uridine(47) in tRNA; Xref=Rhea:RHEA:53364, Rhea:RHEA-COMP:13539, CC Rhea:RHEA-COMP:13540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.89; CC Evidence={ECO:0000250|UniProtKB:Q06053}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53366; CC Evidence={ECO:0000250|UniProtKB:Q06053}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5,6-dihydrouridine(47) in tRNA + NADP(+) = H(+) + NADPH + CC uridine(47) in tRNA; Xref=Rhea:RHEA:53360, Rhea:RHEA-COMP:13539, CC Rhea:RHEA-COMP:13540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.89; CC Evidence={ECO:0000250|UniProtKB:Q06053}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53362; CC Evidence={ECO:0000250|UniProtKB:Q06053}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5,6-dihydrouridine in mRNA + NAD(+) = a uridine in mRNA + CC H(+) + NADH; Xref=Rhea:RHEA:69851, Rhea:RHEA-COMP:14658, Rhea:RHEA- CC COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; CC Evidence={ECO:0000250|UniProtKB:Q9UTH9}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853; CC Evidence={ECO:0000250|UniProtKB:Q9UTH9}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5,6-dihydrouridine in mRNA + NADP(+) = a uridine in mRNA + CC H(+) + NADPH; Xref=Rhea:RHEA:69855, Rhea:RHEA-COMP:14658, Rhea:RHEA- CC COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; CC Evidence={ECO:0000250|UniProtKB:Q9UTH9}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857; CC Evidence={ECO:0000250|UniProtKB:Q9UTH9}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000250|UniProtKB:Q5SMC7}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06053}. Nucleus CC {ECO:0000250|UniProtKB:Q06053}. CC -!- SIMILARITY: Belongs to the Dus family. Dus3 subfamily. {ECO:0000305}. 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; CP000498; ABN66252.1; -; Genomic_DNA. DR RefSeq; XP_001384281.1; XM_001384244.1. DR AlphaFoldDB; A3LUK5; -. DR SMR; A3LUK5; -. DR STRING; 4924.XP_001384281.1; -. DR GeneID; 4838835; -. DR KEGG; pic:PICST_83606; -. DR eggNOG; KOG2333; Eukaryota. DR HOGENOM; CLU_013299_7_3_1; -. DR InParanoid; A3LUK5; -. DR OMA; WSYIAEC; -. DR OrthoDB; 275918at2759; -. DR Proteomes; UP000002258; Chromosome 4. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0102265; F:tRNA-dihydrouridine47 synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR CDD; cd02801; DUS_like_FMN; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR035587; DUS-like_FMN-bd. DR InterPro; IPR018517; tRNA_hU_synthase_CS. DR PANTHER; PTHR45846; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1. DR PANTHER; PTHR45846:SF1; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1. DR Pfam; PF01207; Dus; 1. DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1. DR PROSITE; PS01136; UPF0034; 1. PE 3: Inferred from homology; KW Cytoplasm; Flavoprotein; FMN; Metal-binding; mRNA processing; NAD; NADP; KW Nucleus; Oxidoreductase; Reference proteome; Repeat; tRNA processing; Zinc; KW Zinc-finger. FT CHAIN 1..613 FT /note="tRNA-dihydrouridine(47) synthase [NAD(P)(+)]" FT /id="PRO_0000330247" FT ZN_FING 88..111 FT /note="C3H1-type 1" FT ZN_FING 128..149 FT /note="C3H1-type 2" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 40..78 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 337 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q5SMC7" FT BINDING 250..252 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:Q5SMC7" FT BINDING 305 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:Q5SMC7" FT BINDING 377 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:Q5SMC7" FT BINDING 408 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:Q5SMC7" FT BINDING 456..458 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:Q5SMC7" FT BINDING 480..481 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:Q5SMC7" SQ SEQUENCE 613 AA; 69682 MW; 2F1C257CCA755FB8 CRC64; MTAGEKRTSE ALDQPESKKV HVERGMAAIK PEFIVQKDRI VDSFDDDEAE GGERGVEEGK SGKGGKKKRR GQNKNRDLKQ KREEIRLCTS LLDPDNIKTC AYGPEQCRST HNVEEYLASK PVDIEGICPV FRAIGYCPAG LKCRWLQSHY DKETRKLIKD LGRTEASKIE LNYEVNNVSH EARGKLRKKQ YDFAIAGKVI EYIDSTVQND ENIANAKEQR KNNEATYVDA PYKIAEKKRL DFRNAKIVSP LTTVGNLPYR RLMKKLGADI TYSEMALSVP LLQATNAEWA LPKAHRTEYP GYGVQIATSK HWAAAKVAEI ISRETEHVSE LNLNCGCPID LLYRQGQGSA LLEQPARLVR ILKAMNASSG DIPVTVKIRT GSKENKNTAK TLVERLLAEN DVAAITLHGR SRQQRYTKEA DWNYIAEVGQ VVQQWNDKKE ENKDSRDTQR TCFVGNGDVF SHVDWYNAVN TDGIDSVMVA RGALIKPWIF EEVEAQQYLD KTATERLDIL KTFSDYALEH WGTDEYGVGL ARRFMCEFLS FTHRYIPLGI LERLPPKINE RPPQWKGRNE METLLGSTDY KDWIKITEMF LGKSGDDFVF TPKHKSNSYE KSN //