ID   FOLE_YEAST              Reviewed;         548 AA.
AC   Q08645;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 82.
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=MET7; Synonyms=MET23; OrderedLocusNames=YOR241W; ORFNames=O5248;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   MEDLINE=97127829; PubMed=8972580;
RX   DOI=10.1002/(SICI)1097-0061(199612)12:15<1575::AID-YEA45>3.3.CO;2-5;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   MEDLINE=97313270; PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
RA   Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
RA   Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
RA   Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
RA   Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
RA   Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
RA   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.,
RA   Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
RA   Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
RA   Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
RA   Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
RA   Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
RA   Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
RA   Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
RA   Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
RA   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   [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.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
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   [5]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=20239629; PubMed=10775416; DOI=10.1006/abbi.2000.1741;
RA   DeSouza L., Shen Y., Bognar A.L.;
RT   "Disruption of cytoplasmic and mitochondrial folylpolyglutamate
RT   synthetase activity in Saccharomyces cerevisiae.";
RL   Arch. Biochem. Biophys. 376:299-312(2000).
RN   [6]
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   -!- INTERACTION:
CC       P33203:PRP40; NbExp=1; IntAct=EBI-7058, EBI-701;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm.
CC   -!- MISCELLANEOUS: Present with 7080 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
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DR   EMBL; Z75149; CAA99462.1; -; Genomic_DNA.
DR   EMBL; AY692818; AAT92837.1; -; Genomic_DNA.
DR   PIR; S67134; S67134.
DR   RefSeq; NP_014884.1; -.
DR   HSSP; P15925; 1FGS.
DR   DIP; DIP:4986N; -.
DR   IntAct; Q08645; 20.
DR   PeptideAtlas; Q08645; -.
DR   Ensembl; YOR241W; Saccharomyces cerevisiae.
DR   GeneID; 854415; -.
DR   GenomeReviews; Y13140_GR; YOR241W.
DR   KEGG; sce:YOR241W; -.
DR   NMPDR; fig|4932.3.peg.5996; -.
DR   CYGD; YOR241w; -.
DR   SGD; S000005767; MET7.
DR   HOGENOM; Q08645; -.
DR   OMA; Q08645; GIDHTFM.
DR   BRENDA; 6.3.2.17; 250.
DR   NextBio; 976613; -.
DR   GermOnline; YOR241W; Saccharomyces cerevisiae.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IDA:SGD.
DR   GO; GO:0009396; P:folic acid and derivative biosynthetic process; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon compound metabolic process; IMP:SGD.
DR   InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR   InterPro; IPR001645; Fpolygl_synthtse.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1.
DR   Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
DR   PANTHER; PTHR11136; Fpolygl_synthtse; 1.
DR   Pfam; PF02875; Mur_ligase_C; 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; Mitochondrion;
KW   Nucleotide-binding; One-carbon metabolism.
FT   CHAIN         1    548       Folylpolyglutamate synthase.
FT                                /FTId=PRO_0000168312.
FT   NP_BIND     126    132       ATP (Potential).
SQ   SEQUENCE   548 AA;  62151 MW;  F36811FB4B7E9305 CRC64;
     MHKGKKNYPN LITSFRMNLK KIILNHDRFS HPERWKTNAL LRFTFVYIKF LFDLMIIKNP
     LRMVGKTYRD AVTALNSLQS NYANIMAIRQ TGDRKNTMTL LEMHEWSRRI GYSASDFNKL
     NIVHITGTKG KGSTAAFTSS ILGQYKEQLP RIGLYTSPHL KSVRERIRIN GEPISEEKFA
     KYFFEVWDRL DSTTSSLDKF PHMIPGSKPG YFKFLTLLSF HTFIQEDCKS CVYEVGVGGE
     LDSTNIIEKP IVCGVTLLGI DHTFMLGDTI EEIAWNKGGI FKSGAPAFTV EKQPPQGLTI
     LKERAEERKT TLTEVPPFKQ LENVKLGIAG EFQKSNASLA VMLASEILHT SNILEEKIKC
     SSNASIPEKF IIGLQNTKWE GRCQVLEKGK NVWYIDGAHT KDSMVAASTW FRDMVRLSKR
     KKILLFNQQS RDANALVNNL YSSVSPEITF DDVIFTTNVT WKSGSYSADL VSMNTSQEDV
     EKLKVQESLV KNWNKIDDNR AKTHVTASIE EANELIETLY DEPADIFVTG SLHLVGGLLV
     VFDRIDVK
//