ID   FOLD_YEAST              Reviewed;         427 AA.
AC   Q12676;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 72.
DE   RecName: Full=Folylpolyglutamate synthase;
DE            EC=6.3.2.17;
DE   AltName: Full=Folylpoly-gamma-glutamate synthetase;
DE            Short=FPGS;
DE   AltName: Full=Tetrahydrofolylpolyglutamate synthase;
DE            Short=Tetrahydrofolate synthase;
GN   Name=FOL3; OrderedLocusNames=YMR113W; ORFNames=YM9718.12;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313268; 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.,
RA   Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
RA   Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
RP   CHARACTERIZATION.
RX   MEDLINE=20261521; 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   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923954; 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   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Conversion of folates to polyglutamate derivatives.
CC   -!- CATALYTIC ACTIVITY: ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-
CC       glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1).
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Present with 2340 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
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DR   EMBL; Z49702; CAA89750.1; -; Genomic_DNA.
DR   PIR; S54574; S54574.
DR   RefSeq; NP_013831.1; -.
DR   HSSP; P15925; 1FGS.
DR   Ensembl; YMR113W; Saccharomyces cerevisiae.
DR   GeneID; 855140; -.
DR   GenomeReviews; Z71257_GR; YMR113W.
DR   KEGG; sce:YMR113W; -.
DR   NMPDR; fig|4932.3.peg.4879; -.
DR   CYGD; YMR113w; -.
DR   SGD; S000004719; FOL3.
DR   HOGENOM; Q12676; -.
DR   OMA; Q12676; HPYTHAV.
DR   BRENDA; 6.3.2.17; 250.
DR   NextBio; 978528; -.
DR   ArrayExpress; Q12676; -.
DR   GermOnline; YMR113W; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008841; F:dihydrofolate synthase activity; IMP:SGD.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:EC.
DR   GO; GO:0009396; P:folic acid and derivative biosynthetic process; IMP:SGD.
DR   GO; GO:0006730; P:one-carbon compound metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR   InterPro; IPR001645; Fpolygl_synthtse.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
DR   PANTHER; PTHR11136; Fpolygl_synthtse; 1.
DR   Pfam; PF08245; Mur_ligase_M; 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; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   One-carbon metabolism.
FT   CHAIN         1    427       Folylpolyglutamate synthase.
FT                                /FTId=PRO_0000168308.
FT   NP_BIND      30     36       ATP (Potential).
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
//