ID FOLE_YEAST Reviewed; 548 AA.
AC Q08645; D6W2U3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 01-MAY-2013, entry version 119.
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 (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
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>3.3.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 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 GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RG Saccharomyces Genome Database;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
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 [6]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX 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 [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.,
RA Dephoure N., O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION.
RX PubMed=15161972; DOI=10.1073/pnas.0401263101;
RA Askree S.H., Yehuda T., Smolikov S., Gurevich R., Hawk J., Coker C.,
RA Krauskopf A., Kupiec M., McEachern M.J.;
RT "A genome-wide screen for Saccharomyces cerevisiae deletion mutants
RT that affect telomere length.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8658-8663(2004).
CC -!- FUNCTION: Catalyzes conversion of folates to polyglutamate
CC derivatives allowing concentration of folate compounds in the cell
CC and the intracellular retention of these cofactors, which are
CC important substrates for most of the folate-dependent enzymes that
CC are involved in one-carbon transfer reactions involved in purine,
CC pyrimidine and amino acid synthesis. Required for methionine
CC synthesis and maintenance of intact mitochondrial DNA. Involved in
CC telomere maintenance.
CC -!- CATALYTIC ACTIVITY: ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-
CC glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1).
CC -!- COFACTOR: A monovalent cation (By similarity).
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane
CC (By similarity). Mitochondrion matrix (By similarity). Cytoplasm.
CC -!- DISRUPTION PHENOTYPE: Methionine auxotroph. Undetectable levels of
CC folylpolyglutamate synthase activity. Increased rate of loss of
CC mitochondrial DNA. Respiration-deficient. In combination with
CC deletion of FOL3, the cells are not viable even in the presence of
CC methionine and folinic acid. MET7, FOL3 and TUP1 triple disruption
CC mutant is able to germinate on YPGA medium containing thymidylate
CC and to grow although poorly on synthetic medium containing
CC methionine, adenine and thymidylate. Adenine and thymidine
CC auxotroph when grown in the presence of sulfanilamide. Becomes
CC petite under normal growth conditions but can be maintained with a
CC grande phenotype if the strain is TUP1 and all media are
CC supplemented with dTMP. MET7 GLY1 double mutant is auxotrophic for
CC glycine when grown on glucose but prototrophic when grown on
CC glycerol. MET7 SER1 double mutant cannot use glycine to suppress
CC serine auxotrophy. MET7 SHM2 double mutant is nonviable.
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 EMBL; BK006948; DAA11009.1; -; Genomic_DNA.
DR PIR; S67134; S67134.
DR RefSeq; NP_014884.1; NM_001183660.1.
DR ProteinModelPortal; Q08645; -.
DR SMR; Q08645; 88-404.
DR DIP; DIP-4986N; -.
DR IntAct; Q08645; 9.
DR MINT; MINT-513781; -.
DR STRING; 4932.YOR241W; -.
DR PaxDb; Q08645; -.
DR PeptideAtlas; Q08645; -.
DR EnsemblFungi; YOR241W; YOR241W; YOR241W.
DR GeneID; 854415; -.
DR KEGG; sce:YOR241W; -.
DR CYGD; YOR241w; -.
DR SGD; S000005767; MET7.
DR eggNOG; COG0285; -.
DR GeneTree; ENSGT00390000016526; -.
DR HOGENOM; HOG000181278; -.
DR KO; K01930; -.
DR OMA; MEYQDAI; -.
DR OrthoDB; EOG425928; -.
DR UniPathway; UPA00850; -.
DR NextBio; 976613; -.
DR Genevestigator; Q08645; -.
DR GermOnline; YOR241W; Saccharomyces cerevisiae.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IDA:SGD.
DR GO; GO:0006730; P:one-carbon metabolic process; IMP:SGD.
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; IPR023600; Folylpolyglutamate_synth_euk.
DR InterPro; IPR004101; Mur_ligase_C.
DR InterPro; IPR013221; Mur_ligase_cen.
DR PANTHER; PTHR11136; PTHR11136; 1.
DR PIRSF; PIRSF038895; FPGS; 1.
DR SUPFAM; SSF53244; Mur_ligase_C; 1.
DR SUPFAM; SSF53623; Mur_ligase_cen; 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; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW One-carbon metabolism; Reference proteome.
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
//
