ID K6DCS6_9BACI Unreviewed; 440 AA.
AC K6DCS6;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 ORFNames=BABA_18302 {ECO:0000313|EMBL:EKN65873.1};
OS Neobacillus bataviensis LMG 21833.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN65873.1, ECO:0000313|Proteomes:UP000006316};
RN [1] {ECO:0000313|EMBL:EKN65873.1, ECO:0000313|Proteomes:UP000006316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX PubMed=23087684;
RA Heylen K., Keltjens J.;
RT "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT reduction in Bacillus.";
RL Front. Microbiol. 3:371-371(2012).
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:EKN65873.1}.
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DR EMBL; AJLS01000125; EKN65873.1; -; Genomic_DNA.
DR RefSeq; WP_007086654.1; NZ_AJLS01000125.1.
DR AlphaFoldDB; K6DCS6; -.
DR STRING; 1117379.BABA_18302; -.
DR PATRIC; fig|1117379.3.peg.3790; -.
DR eggNOG; COG0285; Bacteria.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000006316; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006316}.
FT DOMAIN 46..274
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 299..377
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 440 AA; 49184 MW; 5A2BEDB0E0D5EF23 CRC64;
MFTTYKEALD WIHAGLRLGI KPGLKRMEWM MDKLDNPENK IKAVHIGGTN GKGSTVTFLR
SILQAGGYTV GTFTSPYIEQ FNERISINGK PITDDELLQL ANVIRPLADK LEETELGGPT
EFEVITAMAF YYFANIRKPD IVIFEVGLGG RFDSTNIIQP LASIITNIGL DHTNILGNTY
EEIAFEKAGI IKEKTPIFTA VKHSGALKVI EEQADKKSAP IARLNHEFTI SGHNSLTRGE
RFTIETLPHP LKQLEISMIG QHQTENASLA VLAAQYLNEK GFFNITEQSI QSGLKQAYWP
GRFEVLSENP LVIIDGAHNE EGITALTHEL STRFADRNIQ IVFAALADKK LDEMIGKLDK
IANQISFVSF DFPRAAKAEQ LLNISQSNNK LAVDHWQSYL LEEIKNLDVS QMLVVTGSLY
FISEAKPHLC KYLKNKTFSL
//
