ID A0A1Y4SYZ4_9FIRM Unreviewed; 407 AA.
AC A0A1Y4SYZ4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-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=B5E75_04610 {ECO:0000313|EMBL:OUQ35114.1};
OS Massilimicrobiota timonensis.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Massilimicrobiota.
OX NCBI_TaxID=1776392 {ECO:0000313|EMBL:OUQ35114.1, ECO:0000313|Proteomes:UP000195305};
RN [1] {ECO:0000313|Proteomes:UP000195305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An13 {ECO:0000313|Proteomes:UP000195305};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-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}.
CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {ECO:0000256|PIRNR:PIRNR001563}.
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:OUQ35114.1}.
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DR EMBL; NFLJ01000010; OUQ35114.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4SYZ4; -.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000195305; Unassembled WGS sequence.
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; 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 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.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
DR PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 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}.
FT DOMAIN 43..184
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 272..350
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 407 AA; 46505 MW; D1BF94F5D2FCBC55 CRC64;
MFTDVHEAIA YIESKRSKRS IDAFRDTLNK CHILMKQKNM IHIAGTNGKG STVNYLRSIL
NAHGYKVGTF TSPYLICHND RIRVDDIPIS DEDLLKYVNQ YYAIIEEDGL SMFEIDVLIM
LAYFQSLDLD YRIIETGIGG MNDKTNVIDP IVSAITNIGL DHQKQLGDIY DIINEKMGII
KPHQMFITSE TKGTILARFQ EQCDAMGAVM YVVPEYQVSR YPFHFRYRDM AFTLENQGIY
QVTNARLALT IASKLIKLDP IVTQPAIEHA SWKGRYETLD YQGVKVDIDG AHNMPGIKAL
LQTLRVKKEE DVAIVFSCLN DRDVDEMLEA MLKAGYHVYI TTFQDERAID LSSIAPRPHL
TIVNSFIEAM QTAYIKKQHI VVTGSLHFIS RVRKYLIDLQ TQDTKNQ
//
