ID A0A3P5XP19_9BACL Unreviewed; 409 AA.
AC A0A3P5XP19;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=fgs {ECO:0000313|EMBL:VDC32635.1};
GN ORFNames=FILTAD_02836 {ECO:0000313|EMBL:VDC32635.1};
OS Filibacter tadaridae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Filibacter.
OX NCBI_TaxID=2483811 {ECO:0000313|EMBL:VDC32635.1, ECO:0000313|Proteomes:UP000270468};
RN [1] {ECO:0000313|EMBL:VDC32635.1, ECO:0000313|Proteomes:UP000270468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATB-66 {ECO:0000313|EMBL:VDC32635.1};
RA Criscuolo A.;
RL Submitted (NOV-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}.
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DR EMBL; UXAV01000044; VDC32635.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P5XP19; -.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000270468; 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: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:VDC32635.1};
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:UP000270468}.
FT DOMAIN 46..256
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 283..361
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 409 AA; 44559 MW; F61DBAEA7E31585D CRC64;
MIPNMSVYKE RWEIESDDIV KPGVEAVQEA LRKLGNPEQK LNVIHVAGTN GKGSTIAFME
AILKEHGFST GVFSSPAIID IHDQIRIDGN PISEDELNNS FHELKEAGIS GLLTDFELLT
AAAFCTWRRI APDYVLLETG MGGTLDSTNV VTPLVSVITS IALEHSAFLG TTLAEIAGHK
AGIIKNKIPV VIGPMQEESL ETIQRIALEQ ESPLAHYGID LKMEGTEQEV FVGTKTIPLP
TRKMKGPHQG VNAALAIEAL LAAKMDLNGD RVAKAIANAQ LNHRFQEIQP GLFLDGAHNP
AAAKALAKTI QSEFPGEKVD FVMGMIKGKD IKKTLNALMP VAGSFTFLTF SHPQAEQAGH
MIENCSHQHK RVINAVNDTI TLEKRGELKI IVTGSLYLLS SLKYYLKEK
//
