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Database: UniProt
Entry: A8SN77_9FIRM
LinkDB: A8SN77_9FIRM
Original site: A8SN77_9FIRM 
ID   A8SN77_9FIRM            Unreviewed;       425 AA.
AC   A8SN77;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 67.
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:EDP23771.1};
GN   ORFNames=PEPMIC_01577 {ECO:0000313|EMBL:EDP23771.1};
OS   Parvimonas micra ATCC 33270.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Parvimonas.
OX   NCBI_TaxID=411465 {ECO:0000313|EMBL:EDP23771.1, ECO:0000313|Proteomes:UP000003162};
RN   [1] {ECO:0000313|EMBL:EDP23771.1, ECO:0000313|Proteomes:UP000003162}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33270 {ECO:0000313|EMBL:EDP23771.1,
RC   ECO:0000313|Proteomes:UP000003162};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Peptostreptococcus micros (ATCC 33270).";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDP23771.1, ECO:0000313|Proteomes:UP000003162}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33270 {ECO:0000313|EMBL:EDP23771.1,
RC   ECO:0000313|Proteomes:UP000003162};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2007) 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:EDP23771.1}.
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DR   EMBL; ABEE02000017; EDP23771.1; -; Genomic_DNA.
DR   RefSeq; WP_004833543.1; NZ_DS483518.1.
DR   AlphaFoldDB; A8SN77; -.
DR   GeneID; 71955012; -.
DR   eggNOG; COG0285; Bacteria.
DR   HOGENOM; CLU_015869_1_1_9; -.
DR   Proteomes; UP000003162; Unassembled WGS sequence.
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; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
DR   PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR001563};
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..260
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          287..365
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   425 AA;  48013 MW;  5684A18F2FE39E1B CRC64;
     MNYETAMIKL RGEVCSGVKL GLQNIKNLME KLGNPQDKLK IIHIAGTNGK GSCTSFVNSV
     LVSQGYKVGM FTSPSIYNFE ERIRINNKNI PEDKLIELMN EVREIANTLE VFPADFELVT
     ALAFLYFYRE NCDFAIMEVG LGGRLDATNV INKPLITLIT SISFDHQQFL GNTIKEIALE
     KAGIIKDGVP LVLYSQDTEI MDNIMGVAKS KNSKVIVNDL SKIKVLENKK SGQVIDYKDF
     KNLKINLLGS HQVKNATISL ELLLELRKIG FEISNESIYN GFSTVTWPCR FELVSKSPDF
     ILDGAHNIDG IEKFVSNMNF YYKNNKKIAI FGVLADKDYN EMLEKIVPCF DVFLTVRPDS
     ERAMEAYELK EKIEALTEKK VYSFENYQEA IDKAFEISSK DDVISAFGSL YFVGEIRKLL
     GVSDY
//
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