ID A0A2S0UD44_9BACL Unreviewed; 457 AA.
AC A0A2S0UD44;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-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 ORFNames=DCC85_17060 {ECO:0000313|EMBL:AWB45731.1};
OS Paenibacillus sp. CAA11.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1532905 {ECO:0000313|EMBL:AWB45731.1, ECO:0000313|Proteomes:UP000244407};
RN [1] {ECO:0000313|EMBL:AWB45731.1, ECO:0000313|Proteomes:UP000244407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAA11 {ECO:0000313|EMBL:AWB45731.1,
RC ECO:0000313|Proteomes:UP000244407};
RA Um Y., Kim S., Gong G.;
RT "Complete genome of CAA11.";
RL Submitted (APR-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; CP028922; AWB45731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0UD44; -.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000244407; 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: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; 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.
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:UP000244407}.
FT DOMAIN 56..282
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 308..386
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 457 AA; 50812 MW; 0BEE6158C6149886 CRC64;
MGATEEGNSQ PLRSYAEAVD WINGLIPFGI RPGLERIERM LEMLGNPHRK LKFIHVAGTN
GKGSSCAFLT STLLRGGYSV GTFTSPYITK FTNRFQYNGE DIPENTLLGL SNRLYPLVEQ
ITGTELGSPT MFEVSTALAI LYYAEVCYPD VVVWETGLGG RMDVTNIVTP IVCLITNIGM
DHTDILGDTI EQIASEKAGI IKPGVPVVSC AEQPEAIQVF KQTAAAKSST LYLLGEEFSY
ERTGLNGAGQ QFLFKGPFRE LPIEITLQGE HQCKNAAGAM MVLEILRQYM AFVFEDEDIL
NGFKGAAWAG RLELVQDHPR VVLDGAHNPE GAETLARSIP EIYRYRHLNL MMGMLSNKHH
RAYLEHILPI VDTLIVTEPD FRRKMDAEAL AELVQQLREA KAKPTLELIV EPDWREALEL
LRLRTTQEDL GVVSGTLYLI SDVRAALLHQ TDSEKGW
//
