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Database: UniProt
Entry: Q08645
LinkDB: Q08645
Original site: Q08645 
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   16-APR-2014, entry version 128.
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 204508 / S288c;
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. MET7 and FOL3 double
CC       mutant cells are not viable even in the presence of methionine and
CC       folinic acid. MET7, FOL3 and TUP1 triple disruption mutant is able
CC       to germinate on YPGA medium containing thymidylate and to grow
CC       although poorly on synthetic medium containing methionine, adenine
CC       and thymidylate. Adenine and thymidine auxotroph when grown in the
CC       presence of sulfanilamide. Becomes petite under normal growth
CC       conditions but can be maintained with a grande phenotype if the
CC       strain is TUP1 and all media are supplemented with dTMP. MET7 and
CC       GLY1 double mutant is auxotrophic for glycine when grown on
CC       glucose but prototrophic when grown on glycerol. MET7 and SER1
CC       double mutant cannot use glycine to suppress serine auxotrophy.
CC       MET7 and 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; 66-546.
DR   BioGrid; 34632; 110.
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; IPEMVEY; -.
DR   OrthoDB; EOG7GBG5T; -.
DR   BioCyc; YEAST:YOR241W-MONOMER; -.
DR   UniPathway; UPA00850; -.
DR   NextBio; 976613; -.
DR   PRO; PR:Q08645; -.
DR   Genevestigator; Q08645; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
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; SSF53244; 2.
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; 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
//
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