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Database: UniProt
Entry: E2ZKS0_9FIRM
LinkDB: E2ZKS0_9FIRM
Original site: E2ZKS0_9FIRM 
ID   E2ZKS0_9FIRM            Unreviewed;       424 AA.
AC   E2ZKS0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
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   Name=folC {ECO:0000313|EMBL:EFQ06245.1};
GN   ORFNames=HMPREF9436_02273 {ECO:0000313|EMBL:EFQ06245.1};
OS   Faecalibacterium cf. prausnitzii KLE1255.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Faecalibacterium.
OX   NCBI_TaxID=748224 {ECO:0000313|EMBL:EFQ06245.1, ECO:0000313|Proteomes:UP000006028};
RN   [1] {ECO:0000313|EMBL:EFQ06245.1, ECO:0000313|Proteomes:UP000006028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLE1255 {ECO:0000313|EMBL:EFQ06245.1,
RC   ECO:0000313|Proteomes:UP000006028};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00029332};
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|PIRNR:PIRNR001563}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFQ06245.1}.
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DR   EMBL; AECU01000174; EFQ06245.1; -; Genomic_DNA.
DR   RefSeq; WP_005944166.1; NZ_GL538341.1.
DR   AlphaFoldDB; E2ZKS0; -.
DR   STRING; 748224.HMPREF9436_02273; -.
DR   eggNOG; COG0285; Bacteria.
DR   HOGENOM; CLU_015869_1_2_9; -.
DR   OrthoDB; 9809356at2; -.
DR   Proteomes; UP000006028; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:InterPro.
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; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR001563};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001563};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001563}.
FT   DOMAIN          44..262
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          287..364
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   424 AA;  45845 MW;  FE4B073F382A8219 CRC64;
     MNYEQTLEYI HAVQWAGHKP GLTRTRTLLA ALGDPHKQLR FVHVAGTNGK GSTAAMMASC
     LQAAGYRVGL YTSPFINRFN ERIQINGVQI PDEELVKLVE QVKPAADAME DVPTEFEIIT
     ALGMLYFAQQ KCEIVVLEVG LGGTLDSTNV IDAPECAVIT ALGMDHVKEL GPTLADIAAA
     KAGIIKKECP VVSYGGVPEA DIVIRRVCAE KHAELTEVDF SRLKYEGGSL DAVEFDFDGL
     TDVHLPLIGS YQPRNAALAI TALRVMRTHG WNIPENAIRT GLETVSWPGR FELLRHAPAF
     LLDGSHNAHG MRATVQSLRD RFPGQKFVFL VSIMADKDVD QMLSLLAPLA VRFVTVAAHT
     PRAMTAETLA EHIRAYGCRA EAAASIEAGV ARAVELGGEG PVCALGTLYF SGDVRKAFAE
     LVKG
//
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