ID A0A1D3DVE2_9ACTN Unreviewed; 507 AA.
AC A0A1D3DVE2;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=J116_019300 {ECO:0000313|EMBL:OEJ96285.1};
OS Streptomyces thermolilacinus SPC6.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1306406 {ECO:0000313|EMBL:OEJ96285.1, ECO:0000313|Proteomes:UP000095329};
RN [1] {ECO:0000313|EMBL:OEJ96285.1, ECO:0000313|Proteomes:UP000095329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPC6 {ECO:0000313|EMBL:OEJ96285.1,
RC ECO:0000313|Proteomes:UP000095329};
RX PubMed=23868127;
RA Chen X., Zhang B., Zhang W., Wu X., Zhang M., Chen T., Liu G., Dyson P.;
RT "Genome Sequence of Streptomyces violaceusniger Strain SPC6, a Halotolerant
RT Streptomycete That Exhibits Rapid Growth and Development.";
RL Genome Announc. 1:0-0(2013).
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 -!- 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:OEJ96285.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ASHX02000001; OEJ96285.1; -; Genomic_DNA.
DR RefSeq; WP_023588714.1; NZ_ASHX02000001.1.
DR AlphaFoldDB; A0A1D3DVE2; -.
DR STRING; 1306406.J116_019300; -.
DR eggNOG; COG0285; Bacteria.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000095329; 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}.
FT DOMAIN 110..337
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 366..446
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 53597 MW; 29259CA62E0352A5 CRC64;
MSEQPPSSDH PDSDDFADFD DIVEAETTRD PDLAVIEAGS RTLRAQAGPP QGDPVPARPA
DPALDKALRE VEQELSTRWG ETKLEPSVQR IAALMDVLGE PQRAYPSIHI TGTNGKTSTA
RMIEALLGAF DLRTGRYTSP HVQTITERIS LDGAPIDAER FVETYRDIQP YVEMVDGSQE
YRLSFFEVLT GMAYAAFADA PVDVAVVEVG MGGTWDATNV IDASVAVVTP ISLDHTDRLG
TTTAEIAGEK AGIIKQDATV ILAQQPVDAA QVLLKKSVEA DATVAREGME FGVVSREVAV
GGQLLTLRGL GGEYEGVFLP LYGAHQAHNA AVALAAVEAF FGIGAQHARP LDLDTVRRAF
ASVASPGRLE VVRRSPTVVL DAAHNPAGAQ AAAEGVREAF GFSRLIGVVG ASGDKDVRGL
LEAFEPIFAE VVVTANSTPR AMDPDALAAV AVEVFGEERV VVEPRLDDAL EAAITLAEEE
GEFAGAGVLV TGSVITVGEA RLLLRKG
//
