DYR_YEAST
ID DYR_YEAST Reviewed; 211 AA.
AC P07807; D6W2T9;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Dihydrofolate reductase;
DE EC=1.5.1.3;
GN Name=DFR1; OrderedLocusNames=YOR236W; ORFNames=O5231;
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 [GENOMIC DNA].
RX PubMed=2827121; DOI=10.1093/nar/15.24.10355;
RA Lagosky P.A., Taylor G.R., Haynes R.H.;
RT "Molecular characterization of the Saccharomyces cerevisiae dihydrofolate
RT reductase gene (DFR1).";
RL Nucleic Acids Res. 15:10355-10371(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2838385; DOI=10.1016/0378-1119(88)90522-7;
RA Fling M.E., Kopf J., Richards C.A.;
RT "Nucleotide sequence of the dihydrofolate reductase gene of Saccharomyces
RT cerevisiae.";
RL Gene 63:165-174(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2838386; DOI=10.1016/0378-1119(88)90523-9;
RA Barclay B.J., Huang T., Nagel M.G., Misener V.L., Game J.C., Wahl G.M.;
RT "Mapping and sequencing of the dihydrofolate reductase gene (DFR1) of
RT Saccharomyces cerevisiae.";
RL Gene 63:175-185(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8972580;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1575::aid-yea45>3.0.co;2-e;
RA Boyer J., Michaux G., Fairhead C., Gaillon L., Dujon B.;
RT "Sequence and analysis of a 26.9 kb fragment from chromosome XV of the
RT yeast Saccharomyces cerevisiae.";
RL Yeast 12:1575-1586(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [6]
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 [7]
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).
CC -!- FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential
CC reaction for de novo glycine and purine synthesis, and for DNA
CC precursor synthesis (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate +
CC H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00660};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-
CC tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
CC -!- MISCELLANEOUS: Present with 1080 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC {ECO:0000305}.
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DR EMBL; Y00887; CAA68779.1; -; Genomic_DNA.
DR EMBL; M18578; AAB59331.1; -; Genomic_DNA.
DR EMBL; M26668; AAA34564.1; -; Genomic_DNA.
DR EMBL; Z75144; CAA99456.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11005.1; -; Genomic_DNA.
DR PIR; JT0269; RDBYD.
DR RefSeq; NP_014879.1; NM_001183655.1.
DR AlphaFoldDB; P07807; -.
DR SMR; P07807; -.
DR BioGRID; 34628; 469.
DR DIP; DIP-4120N; -.
DR IntAct; P07807; 4.
DR MINT; P07807; -.
DR STRING; 4932.YOR236W; -.
DR BindingDB; P07807; -.
DR ChEMBL; CHEMBL2576; -.
DR DrugCentral; P07807; -.
DR MaxQB; P07807; -.
DR PaxDb; P07807; -.
DR PRIDE; P07807; -.
DR EnsemblFungi; YOR236W_mRNA; YOR236W; YOR236W.
DR GeneID; 854411; -.
DR KEGG; sce:YOR236W; -.
DR SGD; S000005762; DFR1.
DR VEuPathDB; FungiDB:YOR236W; -.
DR eggNOG; KOG1324; Eukaryota.
DR GeneTree; ENSGT00940000168797; -.
DR HOGENOM; CLU_043966_2_1_1; -.
DR InParanoid; P07807; -.
DR OMA; KEMKYFR; -.
DR BioCyc; YEAST:YOR236W-MON; -.
DR UniPathway; UPA00077; UER00158.
DR PRO; PR:P07807; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P07807; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004146; F:dihydrofolate reductase activity; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0046452; P:dihydrofolate metabolic process; IMP:SGD.
DR GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IMP:SGD.
DR CDD; cd00209; DHFR; 1.
DR Gene3D; 3.40.430.10; -; 1.
DR InterPro; IPR012259; DHFR.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR017925; DHFR_CS.
DR InterPro; IPR001796; DHFR_dom.
DR PANTHER; PTHR48069; PTHR48069; 1.
DR Pfam; PF00186; DHFR_1; 1.
DR SUPFAM; SSF53597; SSF53597; 1.
DR PROSITE; PS00075; DHFR_1; 1.
DR PROSITE; PS51330; DHFR_2; 1.
PE 1: Evidence at protein level;
KW NADP; One-carbon metabolism; Oxidoreductase; Reference proteome.
FT CHAIN 1..211
FT /note="Dihydrofolate reductase"
FT /id="PRO_0000186378"
FT DOMAIN 7..210
FT /note="DHFR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00660"
FT BINDING 13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 20..26
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 34..39
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 58..60
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 80..82
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 123..130
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT CONFLICT 27
FT /note="L -> V (in Ref. 1; CAA68779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 211 AA; 24261 MW; E030CDE7DA481D5D CRC64;
MAGGKIPIVG IVACLQPEMG IGFRGGLPWR LPSEMKYFRQ VTSLTKDPNK KNALIMGRKT
WESIPPKFRP LPNRMNVIIS RSFKDDFVHD KERSIVQSNS LANAIMNLES NFKEHLERIY
VIGGGEVYSQ IFSITDHWLI TKINPLDKNA TPAMDTFLDA KKLEEVFSEQ DPAQLKEFLP
PKVELPETDC DQRYSLEEKG YCFEFTLYNR K
