ID A0A2Z6TCV4_9LACO Unreviewed; 417 AA.
AC A0A2Z6TCV4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:GBG04655.1};
GN ORFNames=LrDSM24759_05690 {ECO:0000313|EMBL:GBG04655.1};
OS Lactobacillus rodentium.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=947835 {ECO:0000313|EMBL:GBG04655.1, ECO:0000313|Proteomes:UP000257317};
RN [1] {ECO:0000313|Proteomes:UP000257317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24759 {ECO:0000313|Proteomes:UP000257317};
RA Tanizawa Y., Tohno M., Endo A., Arita M.;
RT "New taxa in the Lactobacillus gasseri group.";
RL Submitted (MAR-2018) 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:GBG04655.1}.
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DR EMBL; BFBY01000003; GBG04655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6TCV4; -.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000257317; 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|ARBA:ARBA00022840, 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000257317}.
FT DOMAIN 44..245
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 284..360
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 417 AA; 47831 MW; D2F19039BD2EC0F2 CRC64;
MKVEEVISKI EHLPKLHEKN DLSYIKKVLA YLGNPQDKVK TIHVTGTNGK GSTSYYIANL
LKKAGKRTGL FVSPYISKFN ERIQINLDLI SDKDLIKAYQ VVTRVINKIK ETDDTFSLVT
FEFETVMAFW LFAEKHCDYA VIEVGIGGQH DKTNVITPEV SVITSIGLDH EDIIGPTIED
IAKEKSGIIK KGRPVVFGEI AAKPLNILIN QAKQMRVRYF EYEKDYQIII DKKIKFTNSQ
YQLSFNLRSP VEAIDMGIAV EVITILGLQL KPQAVEQAIN ETVIPGRYQI ISRHPEIILD
GAHNIQAISN LVGFVREQPH HKLYYLMGMM KDKDLDQVFT QFRFDEEIVL TRIDYPRAAE
FEDFPEFIRN RSQFIENYQA AFDRVKEQLG ENDILIVTGS FYLVGAILNY WEKKDES
//
