FOLD_YEAST
ID FOLD_YEAST Reviewed; 427 AA.
AC Q12676; D6VZT6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Dihydrofolate synthetase;
DE Short=DHFS;
DE EC=6.3.2.12 {ECO:0000305|PubMed:11731153};
GN Name=FOL3; OrderedLocusNames=YMR113W; ORFNames=YM9718.12;
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 CHARACTERIZATION.
RX PubMed=10799479; DOI=10.1074/jbc.275.19.14056;
RA Cherest H., Thomas D., Surdin-Kerjan Y.;
RT "Polyglutamylation of folate coenzymes is necessary for methionine
RT biosynthesis and maintenance of intact mitochondrial genome in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 275:14056-14063(2000).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11731153; DOI=10.1111/j.1574-6968.2001.tb10915.x;
RA Bayly A.M., Berglez J.M., Patel O., Castelli L.A., Hankins E.G., Coloe P.,
RA Hopkins Sibley C., Macreadie I.G.;
RT "Folic acid utilisation related to sulfa drug resistance in Saccharomyces
RT cerevisiae.";
RL FEMS Microbiol. Lett. 204:387-390(2001).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [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: Glutamate-adding enzyme which catalyzes the binding of the
CC first glutamyl side chain to dihydropteroate. Leads to the de nove
CC synthesis of tetrahydrofolate. {ECO:0000269|PubMed:11731153}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydropteroate + ATP + L-glutamate = 7,8-dihydrofolate +
CC ADP + H(+) + phosphate; Xref=Rhea:RHEA:23584, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17839, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57451, ChEBI:CHEBI:456216;
CC EC=6.3.2.12; Evidence={ECO:0000305|PubMed:11731153};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23585;
CC Evidence={ECO:0000305|PubMed:11731153};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2340 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {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; Z49702; CAA89750.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10010.1; -; Genomic_DNA.
DR PIR; S54574; S54574.
DR RefSeq; NP_013831.1; NM_001182613.1.
DR AlphaFoldDB; Q12676; -.
DR SMR; Q12676; -.
DR BioGRID; 35289; 9.
DR IntAct; Q12676; 2.
DR MINT; Q12676; -.
DR STRING; 4932.YMR113W; -.
DR MaxQB; Q12676; -.
DR PaxDb; Q12676; -.
DR PRIDE; Q12676; -.
DR EnsemblFungi; YMR113W_mRNA; YMR113W; YMR113W.
DR GeneID; 855140; -.
DR KEGG; sce:YMR113W; -.
DR SGD; S000004719; FOL3.
DR VEuPathDB; FungiDB:YMR113W; -.
DR eggNOG; KOG2525; Eukaryota.
DR GeneTree; ENSGT00390000016526; -.
DR HOGENOM; CLU_015869_2_0_1; -.
DR InParanoid; Q12676; -.
DR OMA; KCDYAVI; -.
DR BioCyc; YEAST:YMR113W-MON; -.
DR UniPathway; UPA00850; -.
DR PRO; PR:Q12676; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q12676; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008841; F:dihydrofolate synthase activity; IMP:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IMP:SGD.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1190.10; -; 1.
DR Gene3D; 3.90.190.20; -; 1.
DR InterPro; IPR001645; Folylpolyglutamate_synth.
DR InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR PANTHER; PTHR11136; PTHR11136; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR PIRSF; PIRSF001563; Folylpolyglu_synth; 1.
DR SUPFAM; SSF53244; SSF53244; 1.
DR SUPFAM; SSF53623; SSF53623; 1.
DR TIGRFAMs; TIGR01499; folC; 1.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
DR PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; One-carbon metabolism; Reference proteome.
FT CHAIN 1..427
FT /note="Dihydrofolate synthetase"
FT /id="PRO_0000168308"
FT BINDING 34..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08192"
FT BINDING 296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08192"
SQ SEQUENCE 427 AA; 47851 MW; C3307CEF43BE1F30 CRC64;
MAIELGLSRI TKLLEHLGNP QNSLRVLHIA GTNGKGSVCT YLSSVLQQKS YQIGKFTTPH
LVHVTDSITI NNKPIPLERY QNIRLQLEAL NKSHSLKCTE FELLTCTAFK YFYDVQCQWC
VIEVGLGGRL DATNVIPGAN KACCGITKIS LDHESFLGNT LSEISKEKAG IITEGVPFTV
IDGTNEASVI NVVKERCKAL GSELSVTDSQ LNGNMIDTNS WGCFDLAKLP LNGEYQIFNL
RVAMGMLDYL QMNELIDITK NEVSTRLAKV DWPGRLYRMD YRFDKVSNRT VPILMDGAHN
GSAAVELVKY LRKEYGNQPL TFVMAVTHGK NLEPLLQPLL RPIDQVILTR FNNVEGMPWI
HATDPEEIKD FILTQGYTKE IVIENDLHQV LPSLAHVSDE QRRPIVVCGS LYLCGELLRI
HNSHLRN
