ID   F3Y850_MELPT            Unreviewed;       456 AA.
AC   F3Y850;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   02-SEP-2026, entry version 69.
DE   RecName: Full=tetrahydrofolate synthase {ECO:0000256|ARBA:ARBA00013025};
DE            EC=6.3.2.17 {ECO:0000256|ARBA:ARBA00013025};
DE   AltName: Full=Tetrahydrofolylpolyglutamate synthase {ECO:0000256|ARBA:ARBA00030592};
GN   OrderedLocusNames=MPTP_0179 {ECO:0000313|EMBL:BAK20678.1};
OS   Melissococcus plutonius (strain ATCC 35311 / DSM 29964 / CIP 104052 / LMG
OS   20360 / NCIMB 702443).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Melissococcus.
OX   NCBI_TaxID=940190 {ECO:0000313|EMBL:BAK20678.1, ECO:0000313|Proteomes:UP000008456};
RN   [1] {ECO:0000313|EMBL:BAK20678.1, ECO:0000313|Proteomes:UP000008456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB 702443
RC   {ECO:0000313|Proteomes:UP000008456};
RX   PubMed=21622755; DOI=10.1128/JB.05151-11;
RA   Okumura K., Arai R., Okura M., Kirikae T., Takamatsu D., Osaki M.,
RA   Miyoshi-Akiyama T.;
RT   "Complete genome sequence of Melissococcus plutonius ATCC 35311.";
RL   J. Bacteriol. 193:4029-4030(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 35311;
RA   Okumura K., Arai R., Osaki M., Okura M., Kirikae T., Takamatsu D.,
RA   Akiyama T.;
RT   "Whole genome sequence of Melissococcus plutonius ATCC 35311.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + L-glutamate +
CC         ATP = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP +
CC         phosphate + H(+); 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:0000256|ARBA:ARBA00047493};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00008276, ECO:0000256|PIRNR:PIRNR001563}.
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DR   EMBL; AP012200; BAK20678.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3Y850; -.
DR   STRING; 940190.MPTP_0179; -.
DR   KEGG; mps:MPTP_0179; -.
DR   HOGENOM; CLU_015869_1_1_9; -.
DR   Proteomes; UP000008456; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008841; F:dihydrofolate synthase activity; IEA:TreeGrafter.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:UniProtKB-EC.
DR   FunFam; 3.40.1190.10:FF:000011; Folylpolyglutamate synthase/dihydrofolate synthase; 1.
DR   Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   InterPro; IPR001645; Folylpolyglutamate_synth.
DR   InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   NCBIfam; TIGR01499; folC; 1.
DR   PANTHER; PTHR11136:SF0; DIHYDROFOLATE SYNTHETASE-RELATED; 1.
DR   PANTHER; PTHR11136; FOLYLPOLYGLUTAMATE SYNTHASE-RELATED; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   PIRSF; PIRSF001563; Folylpolyglu_synth; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR   PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
DR   PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001563};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001563};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR001563};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008456}.
FT   DOMAIN          64..291
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          321..437
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   456 AA;  51890 MW;  75CE17B30590E048 CRC64;
     MDENKQGIRY NMIKEVKRME LTIEQTLEWL HKRLLFGPRP GLKRVEALLE KLDNPQCKVS
     TIHIAGTNGK GSTVTYLRCM LEELGLKVGT FTSPYIETFN ERISVNGQPI SDEILIKYIK
     KYQPIVASLD QEKETTGITE FEILTALAMD YFLDEAVDIA IIEVGLGGLL DSTNIVHPML
     TAITTIGKDH TEILGDTLEE IAYHKAGIIK QTIPLVTGNI EQAALQSIEQ VAQEKNSPIY
     RYQEEYQINY VGPTKDWQEV FDFYGEMGKL DRLKIPLLGK HQTENAGVAI QLFYLYCQKQ
     SLNFQEKDVY QGLLNAKWPA RMERMSEEPL IIIDGAHNVH AMKQLVENFK REFTGYSVHI
     LFSALATKDI EKMIFYLKQI PNSHLSITSF DYPKVLELST MEKYVDEKTE VVSLWQFGLG
     EILEKMATGD ILLVTGSLYF VSQVRELLLS IGGNNE
//