ID D8FJ27_9FIRM Unreviewed; 318 AA.
AC D8FJ27;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 40.
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};
DE Flags: Fragment;
GN Name=folC {ECO:0000313|EMBL:EFK38916.1};
GN ORFNames=HMPREF9131_1497 {ECO:0000313|EMBL:EFK38916.1};
OS Peptoniphilus sp. oral taxon 836 str. F0141.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=768724 {ECO:0000313|EMBL:EFK38916.1, ECO:0000313|Proteomes:UP000004869};
RN [1] {ECO:0000313|EMBL:EFK38916.1, ECO:0000313|Proteomes:UP000004869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0141 {ECO:0000313|EMBL:EFK38916.1,
RC ECO:0000313|Proteomes:UP000004869};
RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Nelson K.E.;
RT "Genome Sequence of Peptoniphilus sp. oral taxon 836 str. F0141.";
RL Submitted (JUN-2010) 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 -!- 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:EFK38916.1}.
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DR EMBL; AEAA01000093; EFK38916.1; -; Genomic_DNA.
DR RefSeq; WP_009345644.1; NZ_AEAA01000093.1.
DR AlphaFoldDB; D8FJ27; -.
DR Proteomes; UP000004869; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
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; 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; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE 4: Predicted;
FT DOMAIN 44..268
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT NON_TER 318
FT /evidence="ECO:0000313|EMBL:EFK38916.1"
SQ SEQUENCE 318 AA; 36265 MW; 592CD9AFC2FF847E CRC64;
MIYKELIDNI ENRVGKFKSK GNIRMIKILE HFDNPCDSMK FIHIAGTNGK GSTSYFLYEI
LKSKFKVGLY TSPGLTSYRD RIVVGDLRIS QSEFLSIGEE ILEKEKLILD RYGELNKFEF
LTTIAFIYFK RKNCQLVVLE VGMGGRCDST NIIKAENKLI SIITSISYDH MQYLGNTIEE
ISSEKAGIIC QNAIVVTSNK DKKILKVLQD ECKKKNASIY YSKDLCVKIL KSDLQGSKFI
LNLEKKDYEI SLDQIGLYQI ENAILCLYSL FILIKKALID FDFTKATKLI KDAKWKGRMD
LVSKNPRILL DGAHNIGG
//
