Q08645 (FOLE_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Folylpolyglutamate synthase
EC=6.3.2.17

Alternative name(s):
Folylpoly-gamma-glutamate synthetase
Short name=FPGS
Tetrahydrofolylpolyglutamate synthase
Short name=Tetrahydrofolate synthase

Gene names

Name:	MET7
Synonyms:	MET23
Ordered Locus Names:	YOR241W
ORF Names:	O5248

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	548 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis. Required for methionine synthesis and maintenance of intact mitochondrial DNA. Involved in telomere maintenance. Ref.5 Ref.8
Catalytic activity	ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1). Ref.5 Ref.6
Cofactor	A monovalent cation By similarity.
Pathway	Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis.
Subcellular location	Mitochondrion. Mitochondrion inner membrane By similarity. Mitochondrion matrix By similarity. Cytoplasm Ref.6.
Disruption phenotype	Methionine auxotroph. Undetectable levels of folylpolyglutamate synthase activity. Increased rate of loss of mitochondrial DNA. Respiration-deficient. In combination with deletion of FOL3, the cells are not viable even in the presence of methionine and folinic acid. MET7, FOL3 and TUP1 triple disruption mutant is able to germinate on YPGA medium containing thymidylate and to grow although poorly on synthetic medium containing methionine, adenine and thymidylate. Adenine and thymidine auxotroph when grown in the presence of sulfanilamide. Becomes petite under normal growth conditions but can be maintained with a grande phenotype if the strain is TUP1 and all media are supplemented with dTMP. MET7 GLY1 double mutant is auxotrophic for glycine when grown on glucose but prototrophic when grown on glycerol. MET7 SER1 double mutant cannot use glycine to suppress serine auxotrophy. MET7 SHM2 double mutant is nonviable. Ref.5 Ref.6
Miscellaneous	Present with 7080 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Belongs to the folylpolyglutamate synthase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Cellular component	Cytoplasm Membrane Mitochondrion Mitochondrion inner membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	one-carbon metabolic process Inferred from mutant phenotype Ref.6. Source: SGD
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolylpolyglutamate synthase activity Inferred from direct assay Ref.6. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 548	548	Folylpolyglutamate synthase		PRO_0000168312
Regions
	Nucleotide binding	126 – 132	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q08645 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: F36811FB4B7E9305	FASTA	548	62,151
	10 20 30 40 50 60 MHKGKKNYPN LITSFRMNLK KIILNHDRFS HPERWKTNAL LRFTFVYIKF LFDLMIIKNP 70 80 90 100 110 120 LRMVGKTYRD AVTALNSLQS NYANIMAIRQ TGDRKNTMTL LEMHEWSRRI GYSASDFNKL 130 140 150 160 170 180 NIVHITGTKG KGSTAAFTSS ILGQYKEQLP RIGLYTSPHL KSVRERIRIN GEPISEEKFA 190 200 210 220 230 240 KYFFEVWDRL DSTTSSLDKF PHMIPGSKPG YFKFLTLLSF HTFIQEDCKS CVYEVGVGGE 250 260 270 280 290 300 LDSTNIIEKP IVCGVTLLGI DHTFMLGDTI EEIAWNKGGI FKSGAPAFTV EKQPPQGLTI 310 320 330 340 350 360 LKERAEERKT TLTEVPPFKQ LENVKLGIAG EFQKSNASLA VMLASEILHT SNILEEKIKC 370 380 390 400 410 420 SSNASIPEKF IIGLQNTKWE GRCQVLEKGK NVWYIDGAHT KDSMVAASTW FRDMVRLSKR 430 440 450 460 470 480 KKILLFNQQS RDANALVNNL YSSVSPEITF DDVIFTTNVT WKSGSYSADL VSMNTSQEDV 490 500 510 520 530 540 EKLKVQESLV KNWNKIDDNR AKTHVTASIE EANELIETLY DEPADIFVTG SLHLVGGLLV VFDRIDVK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of a 26.9 kb fragment from chromosome XV of the yeast Saccharomyces cerevisiae." Boyer J., Michaux G., Fairhead C., Gaillon L., Dujon B. Yeast 12:1575-1586(1996) [PubMed: 8972580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Polyglutamylation of folate coenzymes is necessary for methionine biosynthesis and maintenance of intact mitochondrial genome in Saccharomyces cerevisiae." Cherest H., Thomas D., Surdin-Kerjan Y. J. Biol. Chem. 275:14056-14063(2000) [PubMed: 10799479] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
[6]	"Disruption of cytoplasmic and mitochondrial folylpolyglutamate synthetase activity in Saccharomyces cerevisiae." DeSouza L., Shen Y., Bognar A.L. Arch. Biochem. Biophys. 376:299-312(2000) [PubMed: 10775416] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"A genome-wide screen for Saccharomyces cerevisiae deletion mutants that affect telomere length." Askree S.H., Yehuda T., Smolikov S., Gurevich R., Hawk J., Coker C., Krauskopf A., Kupiec M., McEachern M.J. Proc. Natl. Acad. Sci. U.S.A. 101:8658-8663(2004) [PubMed: 15161972] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z75149 Genomic DNA. Translation: CAA99462.1. AY692818 Genomic DNA. Translation: AAT92837.1. BK006948 Genomic DNA. Translation: DAA11009.1.
PIR	S67134.
RefSeq	NP_014884.1. NM_001183660.1.
3D structure databases
ProteinModelPortal	Q08645.
SMR	Q08645. Positions 66-546.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4986N.
IntAct	Q08645. 9 interactions.
MINT	MINT-513781.
STRING	Q08645.
Proteomic databases
PeptideAtlas	Q08645.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOR241W; YOR241W; YOR241W.
GeneID	854415.
KEGG	sce:YOR241W.
NMPDR	fig|4932.3.peg.5996.
Organism-specific databases
CYGD	YOR241w.
SGD	S000005767. MET7.
Phylogenomic databases
eggNOG	fuNOG04751.
GeneTree	EFGT00050000004649.
HOGENOM	HBG744947.
OMA	STGNADQ.
OrthoDB	EOG425928.
Gene expression databases
ArrayExpress	Q08645.
Genevestigator	Q08645.
GermOnline	YOR241W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001645. Folylpolyglutamate_synth. IPR018109. Folylpolyglutamate_synth_CS. IPR023600. Folylpolyglutamate_synth_euk. IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. [Graphical view]
Gene3D	G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
KO	K01930.
PANTHER	PTHR11136. Fpolygl_synthtse. 1 hit.
PIRSF	PIRSF038895. FPGS. 1 hit.
SUPFAM	SSF53244. Mur_ligase_C. 1 hit. SSF53623. Mur_ligase_cen. 1 hit.
TIGRFAMs	TIGR01499. FolC. 1 hit.
PROSITE	PS01011. FOLYLPOLYGLU_SYNT_1. 1 hit. PS01012. FOLYLPOLYGLU_SYNT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	976613.

Entry information

Entry name

FOLE_YEAST

Accession

Primary (citable) accession number: Q08645
Secondary accession number(s): D6W2U3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	December 14, 2011
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program