DUS4_YEAST
ID DUS4_YEAST Reviewed; 367 AA.
AC Q06063; D6VZ38;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+];
DE EC=1.3.1.90 {ECO:0000269|PubMed:14970222};
DE AltName: Full=mRNA-dihydrouridine synthase DUS4 {ECO:0000305};
DE EC=1.3.1.- {ECO:0000250|UniProtKB:O74553};
DE AltName: Full=tRNA-dihydrouridine synthase 4;
GN Name=DUS4 {ECO:0000303|PubMed:14970222, ECO:0000312|SGD:S000004397};
GN OrderedLocusNames=YLR405W; ORFNames=L8084.2;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP LEVEL OF 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, AND CATALYTIC ACTIVITY.
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).
CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base
CC found in the D-loop of most tRNAs (PubMed:14970222). Specifically
CC modifies U20a and U20b in cytoplasmic tRNAs (PubMed:14970222). Also
CC able to mediate dihydrouridylation of some mRNAs, thereby affecting
CC their translation (By similarity). {ECO:0000250|UniProtKB:O74553,
CC ECO:0000269|PubMed:14970222}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20a) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(20a) in tRNA; Xref=Rhea:RHEA:53344, Rhea:RHEA-COMP:13535,
CC Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.90;
CC Evidence={ECO:0000269|PubMed:14970222};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53346;
CC Evidence={ECO:0000269|PubMed:14970222};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20a) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(20a) in tRNA; Xref=Rhea:RHEA:53348, Rhea:RHEA-COMP:13535,
CC Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.90;
CC Evidence={ECO:0000269|PubMed:14970222};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53350;
CC Evidence={ECO:0000269|PubMed:14970222};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20b) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(20b) in tRNA; Xref=Rhea:RHEA:53352, Rhea:RHEA-COMP:13537,
CC Rhea:RHEA-COMP:13538, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.90;
CC Evidence={ECO:0000269|PubMed:14970222};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53354;
CC Evidence={ECO:0000269|PubMed:14970222};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20b) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(20b) in tRNA; Xref=Rhea:RHEA:53356, Rhea:RHEA-COMP:13537,
CC Rhea:RHEA-COMP:13538, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.90;
CC Evidence={ECO:0000269|PubMed:14970222};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53358;
CC Evidence={ECO:0000269|PubMed:14970222};
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:O74553};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853;
CC Evidence={ECO:0000250|UniProtKB:O74553};
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:O74553};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857;
CC Evidence={ECO:0000250|UniProtKB:O74553};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q5SMC7};
CC -!- SIMILARITY: Belongs to the Dus family. Dus4 subfamily. {ECO:0000305}.
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DR EMBL; U19729; AAB82341.1; -; Genomic_DNA.
DR EMBL; AY558586; AAS56912.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09704.1; -; Genomic_DNA.
DR PIR; S55961; S55961.
DR RefSeq; NP_013509.1; NM_001182293.1.
DR AlphaFoldDB; Q06063; -.
DR SMR; Q06063; -.
DR BioGRID; 31662; 46.
DR IntAct; Q06063; 1.
DR STRING; 4932.YLR405W; -.
DR iPTMnet; Q06063; -.
DR MaxQB; Q06063; -.
DR PaxDb; Q06063; -.
DR PRIDE; Q06063; -.
DR EnsemblFungi; YLR405W_mRNA; YLR405W; YLR405W.
DR GeneID; 851121; -.
DR KEGG; sce:YLR405W; -.
DR SGD; S000004397; DUS4.
DR VEuPathDB; FungiDB:YLR405W; -.
DR eggNOG; KOG2335; Eukaryota.
DR GeneTree; ENSGT00550000074907; -.
DR HOGENOM; CLU_013299_4_0_1; -.
DR InParanoid; Q06063; -.
DR OMA; FRNCVNT; -.
DR BioCyc; MetaCyc:G3O-32467-MON; -.
DR BioCyc; YEAST:G3O-32467-MON; -.
DR BRENDA; 1.3.1.90; 984.
DR PRO; PR:Q06063; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06063; protein.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IMP:SGD.
DR GO; GO:0102266; F:tRNA-dihydrouridine20a synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IMP: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; IPR001269; DUS_fam.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR Pfam; PF01207; Dus; 1.
DR PIRSF; PIRSF006621; Dus; 1.
DR PROSITE; PS01136; UPF0034; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; mRNA processing; NAD; NADP; Oxidoreductase;
KW Reference proteome; tRNA processing.
FT CHAIN 1..367
FT /note="tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+]"
FT /id="PRO_0000162156"
FT ACT_SITE 128
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 45..47
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 99
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 169
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 197
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 231..233
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 255..256
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
SQ SEQUENCE 367 AA; 41696 MW; 653DFCCF13EAB968 CRC64;
MHTMHIPSGD VLIPKPKLIT EETDPLHIIK TRQKTHGRPV TIAGPMVRYS KLPFRQLCRE
YNVDIVYSPM ILAREYVRNE HARISDLSTN NEDTPLIVQV GVNNVADLLK FVEMVAPYCD
GIGINCGCPI KEQIREGIGC ALIYNSDLLC SMVHAVKDKY GDKLRIETKI RIHEALDETV
ELCRKLCDAG VDWITIHGRT RRTRSSQPAN LDAIKYIIEN ISDKNVPVIA NGDCFKLSDL
ERITKYTGAH GVMAVRGLLS NPALFAGYTT CPWGCIEKFC YWALEFGGLP FQLAQHHLYC
MLENMELKKS LLKKMMNLKN YISLIDWFNK TFEFKRYGED GFGMGVEIPY KANSCVQRSA
SVVERQE
