DUS1_YEAST
ID DUS1_YEAST Reviewed; 423 AA.
AC P53759; D6W0K3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)];
DE EC=1.3.1.88 {ECO:0000269|PubMed:12003496};
DE AltName: Full=mRNA-dihydrouridine synthase DUS1 {ECO:0000305};
DE EC=1.3.1.- {ECO:0000250|UniProtKB:Q9HGN6};
DE AltName: Full=tRNA-dihydrouridine synthase 1;
GN Name=DUS1 {ECO:0000303|PubMed:12003496, ECO:0000312|SGD:S000004545};
GN OrderedLocusNames=YML080W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12003496; DOI=10.1017/s1355838202029825;
RA Xing F., Martzen M.R., Phizicky E.M.;
RT "A conserved family of Saccharomyces cerevisiae synthases effects
RT dihydrouridine modification of tRNA.";
RL RNA 8:370-381(2002).
RN [4]
RP PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION.
RX PubMed=14970222; DOI=10.1074/jbc.m401221200;
RA Xing F., Hiley S.L., Hughes T.R., Phizicky E.M.;
RT "The specificities of four yeast dihydrouridine synthases for cytoplasmic
RT tRNAs.";
RL J. Biol. Chem. 279:17850-17860(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base
CC found in the D-loop of most tRNAs (PubMed:12003496, PubMed:14970222).
CC Specifically modifies U16 and U17 in cytoplasmic tRNAs
CC (PubMed:12003496, PubMed:14970222). Also able to mediate
CC dihydrouridylation of some mRNAs, thereby affecting their translation
CC (By similarity). {ECO:0000250|UniProtKB:Q9HGN6,
CC ECO:0000269|PubMed:12003496, ECO:0000269|PubMed:14970222}.
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; EC=1.3.1.88;
CC Evidence={ECO:0000269|PubMed:12003496};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53378;
CC Evidence={ECO:0000269|PubMed:12003496};
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; EC=1.3.1.88;
CC Evidence={ECO:0000269|PubMed:12003496};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53382;
CC Evidence={ECO:0000269|PubMed:12003496};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(17) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(17) in tRNA; Xref=Rhea:RHEA:53372, Rhea:RHEA-COMP:13541,
CC Rhea:RHEA-COMP:13542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000269|PubMed:12003496};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53374;
CC Evidence={ECO:0000269|PubMed:12003496};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(17) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(17) in tRNA; Xref=Rhea:RHEA:53368, Rhea:RHEA-COMP:13541,
CC Rhea:RHEA-COMP:13542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000269|PubMed:12003496};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53370;
CC Evidence={ECO:0000269|PubMed:12003496};
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:Q9HGN6};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853;
CC Evidence={ECO:0000250|UniProtKB:Q9HGN6};
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:Q9HGN6};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857;
CC Evidence={ECO:0000250|UniProtKB:Q9HGN6};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q5SMC7};
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P53759; P39940: RSP5; NbExp=2; IntAct=EBI-27885, EBI-16219;
CC -!- SIMILARITY: Belongs to the Dus family. Dus1 subfamily. {ECO:0000305}.
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DR EMBL; Z46373; CAA86498.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09817.1; -; Genomic_DNA.
DR PIR; S48817; S48817.
DR RefSeq; NP_013631.1; NM_001182439.1.
DR AlphaFoldDB; P53759; -.
DR SMR; P53759; -.
DR BioGRID; 35061; 66.
DR IntAct; P53759; 3.
DR STRING; 4932.YML080W; -.
DR iPTMnet; P53759; -.
DR MaxQB; P53759; -.
DR PaxDb; P53759; -.
DR PRIDE; P53759; -.
DR EnsemblFungi; YML080W_mRNA; YML080W; YML080W.
DR GeneID; 854895; -.
DR KEGG; sce:YML080W; -.
DR SGD; S000004545; DUS1.
DR VEuPathDB; FungiDB:YML080W; -.
DR eggNOG; KOG2335; Eukaryota.
DR GeneTree; ENSGT00550000075089; -.
DR HOGENOM; CLU_013299_5_1_1; -.
DR InParanoid; P53759; -.
DR OMA; VKQYPPC; -.
DR BioCyc; MetaCyc:G3O-32671-MON; -.
DR BioCyc; YEAST:G3O-32671-MON; -.
DR BRENDA; 1.3.1.88; 984.
DR PRO; PR:P53759; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P53759; protein.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IDA:SGD.
DR GO; GO:0102263; F:tRNA-dihydrouridine17 synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IDA:SGD.
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; IPR018517; tRNA_hU_synthase_CS.
DR Pfam; PF01207; Dus; 1.
DR PROSITE; PS01136; UPF0034; 1.
PE 1: Evidence at protein level;
KW Acetylation; Flavoprotein; FMN; mRNA processing; NAD; NADP; Oxidoreductase;
KW Reference proteome; tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..423
FT /note="tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]"
FT /id="PRO_0000162153"
FT REGION 404..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 121
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 35..37
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 92
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 160
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 188
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 223..225
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 247..248
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 423 AA; 48131 MW; 7D226E166CE42F43 CRC64;
MTEPALSSAN NALMQKLTGR QLFDKIGRPT RIVAPMVDQS ELAWRILSRR YGATLAYTPM
LHAKLFATSK KYREDNWSSL DGSSVDRPLV VQFCANDPEY LLAAAKLVED KCDAVDLNLG
CPQGIAKKGH YGSFLMEEWD LIHNLINTLH KNLKVPVTAK IRIFDDCEKS LNYAKMVLDA
GAQFLTVHGR VREQKGQKTG LANWETIKYL RDNLPKETVF FANGNILYPE DISRCMEHIG
ADAVMSAEGN LYNPGVFNVG QTKNKEKIFP RVDKIIREYF QIVKECQESK ASKTAMKSHF
FKILRPFLPH HTDIRSTLAT MNAKATWEEW EEQVVKPVEK VVQEIFEQPD IAIKDEITIG
EKQSWGGSYR TVPYWRCQPY FRPVNGITGD KRVMQGLIDE SVNKKRKADV PLESADKKKD
VKA
