ID B1MXE8_LEUCK Unreviewed; 393 AA.
AC B1MXE8;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
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=folC1 {ECO:0000313|EMBL:ACA82200.1};
GN OrderedLocusNames=LCK_00367 {ECO:0000313|EMBL:ACA82200.1};
OS Leuconostoc citreum (strain KM20).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=349519 {ECO:0000313|EMBL:ACA82200.1, ECO:0000313|Proteomes:UP000002166};
RN [1] {ECO:0000313|EMBL:ACA82200.1, ECO:0000313|Proteomes:UP000002166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KM20 {ECO:0000313|EMBL:ACA82200.1,
RC ECO:0000313|Proteomes:UP000002166};
RX PubMed=18281406; DOI=10.1128/JB.01862-07;
RA Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT "Complete genome sequence of Leuconostoc citreum KM20.";
RL J. Bacteriol. 190:3093-3094(2008).
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};
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DR EMBL; DQ489736; ACA82200.1; -; Genomic_DNA.
DR RefSeq; WP_004907386.1; NC_010471.1.
DR AlphaFoldDB; B1MXE8; -.
DR STRING; 349519.LCK_00367; -.
DR KEGG; lci:LCK_00367; -.
DR eggNOG; COG0285; Bacteria.
DR HOGENOM; CLU_015869_1_1_9; -.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000002166; Chromosome.
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:UniProtKB-EC.
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; 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; PF08245; Mur_ligase_M; 1.
DR PIRSF; PIRSF001563; Folylpolyglu_synth; 2.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000313|EMBL:ACA82200.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840}.
FT DOMAIN 46..194
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 393 AA; 43167 MW; C8111BAC626D1193 CRC64;
MKTVEDAITF IHSRPKGGQK ESLHRMFTLL NALDNPQEQL PPAIHVTGTN GKGSVSTMAS
NILRVAGYRT GLFISPYIVN FRERIQINNQ WIAEQDLLEV AQLVEKKLIT VDQQLAPDVP
TEFEVLTAIM MTYFARENLD ALVIEVGIGG QLDSTNVMPN ATVAVITSVG LDHQALLGDT
IAAIAEQKAG IIHDNMAVVI GELPEAAQWV IEKRSKRPLI HGHSGQFEQG LPGQYQVQNT
ATAVAAVNAF DESITVEQIQ NGLKQSQFAA RFETIRPGII IDGAHNYQGL MQLVTALNTG
EYEKQTKTLI IGSLMDKNVV LAFSDILTQT KFDIVLVPFT GPNGRHSLNI SSVAKQYAIK
TADSWQTAFH ESHSDMTIFT GSLYFVSEVR NQL
//
