ID   FOLE_CANAX              Reviewed;         514 AA.
AC   Q9Y893;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 85.
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;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Subramanian M., Li C., DeSouza L., Bognar A.L.;
RT   "Sequencing of a Candida albicans genomic library plasmid which encodes the
RT   complete open reading frame of folylpolyglutamate synthetase.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
CC         Evidence={ECO:0000250};
CC       Note=A monovalent cation. {ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
CC       Mitochondrion matrix {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AF156928; AAD40312.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Y893; -.
DR   SMR; Q9Y893; -.
DR   VEuPathDB; FungiDB:C2_04380C_A; -.
DR   VEuPathDB; FungiDB:CAWG_04194; -.
DR   UniPathway; UPA00850; -.
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..514
FT                   /note="Folylpolyglutamate synthase"
FT                   /id="PRO_0000168309"
FT   BINDING         82..85
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   BINDING         107
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   BINDING         186
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   BINDING         214
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   BINDING         339
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   BINDING         355
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
SQ   SEQUENCE   514 AA;  57908 MW;  EA8F3C8CCC79A12A CRC64;
     MNQTTETDSM RINLQRTYKD AINALNSLQS NFASIEATKK LGPSVNRNEL SINEVHEFTK
     RLGYTPTDFN KLNIIHITGT KGKGSTCAFT ESILKQYTIS KIGLYTSPHL KSVRERIRIN
     GQPINQEKFA KYFFEVWDKF TTTKSDPQEC PTLQPCDQVK PMYFKYLTIL SFHVFLQEGV
     DTAIYEVGVG GTYDSTNIID KPTVTGISAL GIDHTFMLGN NIASITENKT GIFKKGVPAF
     VSRQLEYPET HELIEKRAKQ LGVSSLEFVD TEDLPNVKLG LSGEFQKQNA ALAIRIANSH
     LKTIGITQDL PEFNNNDGKI KKLSNKFIKG LENVDWPGRC QIINNNPTGI TWYIDGAHTI
     ESINASSTWF KQEQIKLEKP KRRALLFNQQ GRENYAELLE KLFNVTYGTG SEPQIKFDDV
     IFTTNTTWSS GQFNSELISK NTSEDAVKKL EVQNNLSEVW RKLDGGVSKR HVFADIETAV
     NYLKDLGDKD LQVFVCGSLH LVGGFLVVLD NERD