ID B1HVC7_LYSSC Unreviewed; 416 AA.
AC B1HVC7;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
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:ACA41429.1};
GN OrderedLocusNames=Bsph_3961 {ECO:0000313|EMBL:ACA41429.1};
OS Lysinibacillus sphaericus (strain C3-41).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=444177 {ECO:0000313|EMBL:ACA41429.1, ECO:0000313|Proteomes:UP000002164};
RN [1] {ECO:0000313|EMBL:ACA41429.1, ECO:0000313|Proteomes:UP000002164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3-41 {ECO:0000313|EMBL:ACA41429.1,
RC ECO:0000313|Proteomes:UP000002164};
RX PubMed=18296527; DOI=10.1128/JB.01652-07;
RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA Berry C., Yuan Z.;
RT "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT sphaericus C3-41 and comparison with those of closely related Bacillus
RT species.";
RL J. Bacteriol. 190:2892-2902(2008).
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}.
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DR EMBL; CP000817; ACA41429.1; -; Genomic_DNA.
DR RefSeq; WP_012295473.1; NC_010382.1.
DR AlphaFoldDB; B1HVC7; -.
DR EnsemblBacteria; ACA41429; ACA41429; Bsph_3961.
DR KEGG; lsp:Bsph_3961; -.
DR HOGENOM; CLU_015869_1_1_9; -.
DR Proteomes; UP000002164; Chromosome.
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:UniProtKB-EC.
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 Ligase {ECO:0000256|PIRNR:PIRNR001563, ECO:0000313|EMBL:ACA41429.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001563}.
FT DOMAIN 47..263
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 298..365
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 416 AA; 45635 MW; C70079241D06D4A2 CRC64;
MIPGFNHYKE KWAVHSDDVI KPGLVAMEEA LLLVGNPQQA LHVVHLAGTN GKGSTLTFLE
ALAKEHTLRV GKFMSPCIVD VHDQIQIDGQ PITEADMDAV FRQMHAAGLS GKLTDFELLT
VAAFLYFVNN DVDLSLIEAG MGGLLDSTNV VIPIVSIIPS IALEHTQFLG NTIDSIARHK
AGIIKQNRPV IIGNLPEDAK RVVYAEATQK KANVYEIGQH FSISSSTEGE YYLNDGRNVQ
FSHLTRSMKG PHQANNMALA ISAFLEVAAF FNVPVKKTAV REAVKKAAIL GRFEEIIPFV
IVDGAHNPAS AETLVETIKN EFPGEQITFV VGILADKDVQ QILRLLEQVS DEFYFVDFDN
PRAMAAQNLL GLSKATSKNI LVDYVQFLQV QSDSKRRTVV SGSLYLLTAV RNSLKV
//
