ID A0A3G8JFY0_9ACTN Unreviewed; 548 AA.
AC A0A3G8JFY0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-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 Name=folC {ECO:0000313|EMBL:AZG43987.1};
GN ORFNames=D7316_00567 {ECO:0000313|EMBL:AZG43987.1};
OS Gordonia insulae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=2420509 {ECO:0000313|EMBL:AZG43987.1, ECO:0000313|Proteomes:UP000271469};
RN [1] {ECO:0000313|EMBL:AZG43987.1, ECO:0000313|Proteomes:UP000271469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS17-SY073 {ECO:0000313|EMBL:AZG43987.1,
RC ECO:0000313|Proteomes:UP000271469};
RA Kim Y.S., Kim S.B.;
RT "Gordonia insulae sp. nov., isolated from an island soil.";
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}.
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DR EMBL; CP033972; AZG43987.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G8JFY0; -.
DR KEGG; gom:D7316_00567; -.
DR Proteomes; UP000271469; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008841; F:dihydrofolate synthase activity; IEA:UniProtKB-EC.
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 Ligase {ECO:0000313|EMBL:AZG43987.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000271469}.
FT DOMAIN 224..376
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 403..481
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 57935 MW; 32EAB3DA7B73937E CRC64;
MSRDDLGIGP DSDDIPDDLD RDHLGPDPRR RNELDVDPLG AAPLPTDLGS LLAGRGGAPD
ELYADDVAMD DEEDRRAAPA DPGPRDDAAT LAELADLETE LDTRWPETRI EPSLTRISAL
MDLLGSPQHS YPAIHIAGTN GKTSVARMID ALLIAMHRRT GRITSPHLQR VTERISVDGK
PISARTYIDT YRDLEPYITM VDDSSTAAGG PRMSKFEVLT AMSYAVFAEA PVDVAVVETG
MGGRWDATNV IDATVAVITP IAMDHADYLG DTLAAIASEK AGIIKKADPD DLVPTDPVTI
LAVQEPEVAE VLLRQAVESE TLVARENSEF AVLESATAVG GQLLRLQGLG GVYDEIYLPL
HGAHQASNAA IALAAVEAFF GAGADRQLDV EAIRAGFAAV ESPGRLERVR GAPTVFVDAA
HNPHGAAALA QALAEEFDFR RLVGVIGMLG DKDAEGFLEA VEPVFDTIVL TNNGSPRALD
TETLAEIARP IYGEDRVVVE PFLPDAVEVA IGLAEQSDGE PVSGAGVVIT GSVVTAGAAR
TLFGKEPS
//
