ID   FOLE_YEAS7              Reviewed;         548 AA.
AC   A6ZP80;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Folylpolyglutamate synthase {ECO:0000250|UniProtKB:Q08645, ECO:0000312|EMBL:EDN63570.1};
DE            EC=6.3.2.17 {ECO:0000250|UniProtKB:Q08645};
DE   AltName: Full=Folylpoly-gamma-glutamate synthetase {ECO:0000250|UniProtKB:Q08645};
DE            Short=FPGS {ECO:0000250|UniProtKB:Q08645};
DE   AltName: Full=Tetrahydrofolylpolyglutamate synthase {ECO:0000250|UniProtKB:Q08645};
DE            Short=Tetrahydrofolate synthase {ECO:0000250|UniProtKB:Q08645};
GN   Name=MET7; ORFNames=SCY_5295;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1] {ECO:0000312|EMBL:EDN63570.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Catalyzes conversion of folates to polyglutamate derivatives
CC       allowing concentration of folate compounds in the cell and the
CC       intracellular retention of these cofactors, which are important
CC       substrates for most of the folate-dependent enzymes that are involved
CC       in one-carbon transfer reactions involved in purine, pyrimidine and
CC       amino acid synthesis. Required for methionine synthesis and maintenance
CC       of intact mitochondrial DNA. Involved in telomere maintenance (By
CC       similarity). {ECO:0000250|UniProtKB:Q08645}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-
CC         glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP +
CC         H(+) + phosphate; Xref=Rhea:RHEA:10580, Rhea:RHEA-COMP:14738,
CC         Rhea:RHEA-COMP:14740, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:141005,
CC         ChEBI:CHEBI:456216; EC=6.3.2.17;
CC         Evidence={ECO:0000250|UniProtKB:Q08645};
CC   -!- COFACTOR:
CC       Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
CC         Evidence={ECO:0000250|UniProtKB:Q08645};
CC       Note=A monovalent cation. {ECO:0000250|UniProtKB:Q08645};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC       biosynthesis. {ECO:0000250|UniProtKB:Q08645}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q08645}. Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q08645}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q08645}.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000250|UniProtKB:Q08645}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFW02000032; EDN63570.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZP80; -.
DR   SMR; A6ZP80; -.
DR   EnsemblFungi; EDN63570; EDN63570; SCY_5295.
DR   HOGENOM; CLU_015869_0_1_1; -.
DR   UniPathway; UPA00850; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
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; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   PANTHER; PTHR11136; PTHR11136; 1.
DR   PANTHER; PTHR11136:SF5; PTHR11136:SF5; 1.
DR   PIRSF; PIRSF038895; FPGS; 1.
DR   SUPFAM; SSF53244; SSF53244; 1.
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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Magnesium; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW   One-carbon metabolism.
FT   CHAIN           1..548
FT                   /note="Folylpolyglutamate synthase"
FT                   /id="PRO_0000414495"
FT   BINDING         130..133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   BINDING         157
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   BINDING         234
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   BINDING         262
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   BINDING         382
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   BINDING         396
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
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