ID   FOLC_DICDI              Reviewed;         626 AA.
AC   Q54CY5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Putative folylpolyglutamate synthase;
DE            EC=6.3.2.17;
DE   AltName: Full=Folylpoly-gamma-glutamate synthetase;
DE            Short=FPGS;
DE   AltName: Full=Tetrahydrofolate synthase;
DE   AltName: Full=Tetrahydrofolylpolyglutamate synthase;
GN   Name=folC; ORFNames=DDB_G0292632;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Conversion of folates to polyglutamate derivatives.
CC       {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   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC       biosynthesis.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000194; EAL61119.1; -; Genomic_DNA.
DR   RefSeq; XP_629535.1; XM_629533.1.
DR   AlphaFoldDB; Q54CY5; -.
DR   SMR; Q54CY5; -.
DR   STRING; 44689.DDB0230134; -.
DR   PaxDb; Q54CY5; -.
DR   EnsemblProtists; EAL61119; EAL61119; DDB_G0292632.
DR   GeneID; 8628793; -.
DR   KEGG; ddi:DDB_G0292632; -.
DR   dictyBase; DDB_G0292632; folC.
DR   eggNOG; KOG2525; Eukaryota.
DR   HOGENOM; CLU_015869_0_2_1; -.
DR   InParanoid; Q54CY5; -.
DR   OMA; RNTCANY; -.
DR   PhylomeDB; Q54CY5; -.
DR   Reactome; R-DDI-196757; Metabolism of folate and pterines.
DR   UniPathway; UPA00850; -.
DR   PRO; PR:Q54CY5; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046901; P:tetrahydrofolylpolyglutamate biosynthetic process; IBA:GO_Central.
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   SUPFAM; SSF53244; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
DR   TIGRFAMs; TIGR01499; folC; 1.
DR   PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   One-carbon metabolism; Reference proteome.
FT   CHAIN           1..626
FT                   /note="Putative folylpolyglutamate synthase"
FT                   /id="PRO_0000339187"
FT   BINDING         144..147
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   BINDING         168
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   BINDING         235
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   BINDING         263
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   BINDING         412
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
FT   BINDING         430
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P08192"
SQ   SEQUENCE   626 AA;  70637 MW;  8E97F63F6963F1F3 CRC64;
     MNKILLKRQI LYNLPKYFKN NIPYTITINK SNQFINNNCK NNNNNFRKLN FTTTTTTTTT
     APITNNKPKS NMLYSPKDRS YEEAVNALLT LQSNQTVIIS WTKERRDNKE ESAKFLMEEM
     RNYCKTLSID LERESIIHVA GTKGKGSTCA ITESIIREQG FSTGLFTSPH LISPRERIRI
     NGEMISKEMF SQYFWNCWDL LIKDYQTQLP NFFRYLTLMA LKIFQDEAIQ CTILEVGIGG
     RMDSTNVFPK PMVTGISALG YDHQNLLGNT LAEIALEKAG IMKVGIPIFT VSSQLPEAIN
     VLIDHSNKVK SPLSIVPSID QYTISSGGGN NNNNKIESIG LKGTHQLENA SLAIALANCW
     FKKQTFKDVN EIFNSENHKQ YNYETNNYNV TQFTPLLKSI ELGLKNCEWA GRAQHFTNPS
     HFPNMDFYLD GAHTVESSIV MLNWWKSIVN TTTTTTTTTT TTTTNNNDDD TIHILIFNST
     GGRNPTSFLT PIIQSIDNKE IPIFNKSIIP NIIIEKPIDK KYYINEIIQS NQSSTATTTP
     IPDNAAVKQT TEIKESSTWE DFVVECYDKL SKKSHPCITA DSIESSIEIA KELSENGTKN
     VKVLITGSLY LVGGVLKVLL KEKSFN