ID   A0A1H5BDI7_9ACTN        Unreviewed;       495 AA.
AC   A0A1H5BDI7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=SAMN05216489_03685 {ECO:0000313|EMBL:SED52669.1};
OS   Streptomyces sp. 3213.3.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1855348 {ECO:0000313|EMBL:SED52669.1, ECO:0000313|Proteomes:UP000198754};
RN   [1] {ECO:0000313|EMBL:SED52669.1, ECO:0000313|Proteomes:UP000198754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3213 {ECO:0000313|EMBL:SED52669.1,
RC   ECO:0000313|Proteomes:UP000198754};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNTK01000001; SED52669.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5BDI7; -.
DR   STRING; 1855348.SAMN05216489_03685; -.
DR   Proteomes; UP000198754; 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; 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   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   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198754}.
FT   DOMAIN          98..325
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          354..433
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   495 AA;  52421 MW;  ADC40B3CE77DA9B9 CRC64;
     MTDSDPFDEI IEAETDRDPD LAVIEAGSRT LRTQGTGAPQ ADVPGRPEDP QLDAALREVE
     AELATRWGET KLEPSVSRIA ALMDVLGDPQ RSYPSIHITG TNGKTSTARM IEALLGAFEL
     RTGRYTSPHV QSITERISLD GAPISAERFI ETYDDIKPYI EMVDAQQEFR LSFFEVLTGM
     AYAAFADAPV DVAVVEVGMG GTWDATNVID ADVAVVTPID LDHTDRLGGT TGEIAAEKAG
     IVKQDATVIL AQQPVDAAQV LLKKAVEVDA TVAREGLEFG VVSRNVAVGG QLIDLRGLGG
     EYEEIYLPLH GPYQAHNAAV ALAAVEAFFG VGAQRPDPLA IDTVRKAFAS VTSPGRLEVV
     RRSPTVVLDA AHNPAGARAT AEAVAEAFDF SRLIGVVGAS GDKNVRGLLE AFEPMFAEVV
     VTQNSSHRAM DADELAAIAV EVFGDERVQV EPRLPDALEA AITLAEEDGE FAGGGVLVTG
     SVITVGEARL LLGRG
//