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 02-DEC-2020, entry version 86. DE RecName: Full=tRNA-dihydrouridine(47) synthase [NAD(P)(+)]; DE EC=1.3.1.89; 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). {ECO:0000250}. 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 -!- 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 -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000250|UniProtKB:Q5SMC7}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. 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 STRING; 4924.XP_001384281.1; -. DR EnsemblFungi; ABN66252; ABN66252; PICST_83606. DR GeneID; 4838835; -. DR KEGG; pic:PICST_83606; -. DR eggNOG; KOG2333; Eukaryota. DR HOGENOM; CLU_013299_7_3_1; -. DR InParanoid; A3LUK5; -. DR OMA; IAANKPW; -. DR OrthoDB; 1016307at2759; -. DR Proteomes; UP000002258; Chromosome 4. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0034399; C:nuclear periphery; IEA:EnsemblFungi. 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 CDD; cd02801; DUS_like_FMN; 1. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR035587; DUS-like_FMN-bd. DR InterPro; IPR001269; tRNA_hU_synthase. DR InterPro; IPR018517; tRNA_hU_synthase_CS. DR Pfam; PF01207; Dus; 1. DR PROSITE; PS01136; UPF0034; 1. PE 3: Inferred from homology; KW Cytoplasm; Flavoprotein; FMN; Metal-binding; NAD; NADP; Nucleus; KW 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 NP_BIND 250..252 FT /note="FMN" FT /evidence="ECO:0000250|UniProtKB:Q5SMC7" FT NP_BIND 456..458 FT /note="FMN" FT /evidence="ECO:0000250|UniProtKB:Q5SMC7" FT NP_BIND 480..481 FT /note="FMN" FT /evidence="ECO:0000250|UniProtKB:Q5SMC7" FT ACT_SITE 337 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q5SMC7" FT BINDING 305 FT /note="FMN" FT /evidence="ECO:0000250|UniProtKB:Q5SMC7" FT BINDING 377 FT /note="FMN" FT /evidence="ECO:0000250|UniProtKB:Q5SMC7" FT BINDING 408 FT /note="FMN" 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 //