ID A0A238UML0_9ACTN Unreviewed; 475 AA.
AC A0A238UML0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=SAMN06265355_10128 {ECO:0000313|EMBL:SNR22723.1};
OS Actinomadura mexicana.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=134959 {ECO:0000313|EMBL:SNR22723.1, ECO:0000313|Proteomes:UP000198420};
RN [1] {ECO:0000313|EMBL:SNR22723.1, ECO:0000313|Proteomes:UP000198420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44485 {ECO:0000313|EMBL:SNR22723.1,
RC ECO:0000313|Proteomes:UP000198420};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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}.
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DR EMBL; FZNP01000001; SNR22723.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238UML0; -.
DR Proteomes; UP000198420; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 2.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE 4: Predicted;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 54..281
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 331..409
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 475 AA; 49628 MW; F93201763F8F296C CRC64;
MTVSQVSEPS DYRATVGAIM GRGVEWEIDP ALDRIADLVD VLGGPHRAYP VIHIAGTNGK
STTARLVEAL LRERGLRTGL YTSPELTTLR ERIAIDGEPI SEERFVEAYE DVLPYLQLVD
DKHEARLSFF EVLTAMAFAA FADAPVDVAV VEAGMGGSWD ATNVADGAVA VITPIGLDHT
GYLGDTLEQI AGEKAGIIKP GAIAVLSQQP VEAAEVLLRR VVETGAAAAR EGVEYGVLGR
DVAFGGQQIS LRGLHGVYDE IFLPLFGEHQ ASNAATALAA VEAFAGGAPT RGEPNLEAAT
RVAPGETFLG GEEGQLDPAL VRSGFAKSAS PGRLEVARTG PTVLLDAAHN PAGMAATVAT
VTESFGFTRL AGVLAIAADK DVAGVLDQLE PVLAELVVTR NSSARSMPPE ELAEIAEGIF
GAERVHVVQR LDDAIDRAIG LAEETGEYRG AGVLITGSVV TAGDARTLLR VGEGR
//
