ID FTHS_LACPL Reviewed; 551 AA. AC Q88W76; F9UPC7; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 102. DE RecName: Full=Formate--tetrahydrofolate ligase {ECO:0000255|HAMAP-Rule:MF_01543}; DE EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543}; DE AltName: Full=Formyltetrahydrofolate synthetase {ECO:0000255|HAMAP-Rule:MF_01543}; DE Short=FHS {ECO:0000255|HAMAP-Rule:MF_01543}; DE Short=FTHFS {ECO:0000255|HAMAP-Rule:MF_01543}; GN Name=fhs {ECO:0000255|HAMAP-Rule:MF_01543}; OrderedLocusNames=lp_1779; OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) OS (Lactobacillus plantarum). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactiplantibacillus. OX NCBI_TaxID=220668; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; RX PubMed=12566566; DOI=10.1073/pnas.0337704100; RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P., RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J., RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M., RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M., RA Siezen R.J.; RT "Complete genome sequence of Lactobacillus plantarum WCFS1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; RX PubMed=22156394; DOI=10.1128/jb.06275-11; RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M., RA Kleerebezem M., van Hijum S.A.; RT "Complete resequencing and reannotation of the Lactobacillus plantarum RT WCFS1 genome."; RL J. Bacteriol. 194:195-196(2012). CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-10- CC formyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:20221, CC ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57453, ChEBI:CHEBI:195366, ChEBI:CHEBI:456216; CC EC=6.3.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01543}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000255|HAMAP-Rule:MF_01543}. CC -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family. CC {ECO:0000255|HAMAP-Rule:MF_01543}. 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; AL935263; CCC79066.1; -; Genomic_DNA. DR RefSeq; WP_011101546.1; NC_004567.2. DR RefSeq; YP_004889580.1; NC_004567.2. DR AlphaFoldDB; Q88W76; -. DR SMR; Q88W76; -. DR STRING; 220668.lp_1779; -. DR EnsemblBacteria; CCC79066; CCC79066; lp_1779. DR KEGG; lpl:lp_1779; -. DR PATRIC; fig|220668.9.peg.1500; -. DR eggNOG; COG2759; Bacteria. DR HOGENOM; CLU_003601_3_3_9; -. DR OrthoDB; 9761733at2; -. DR PhylomeDB; Q88W76; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000000432; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR CDD; cd00477; FTHFS; 1. DR Gene3D; 3.30.1510.10; Domain 2, N(10)-formyltetrahydrofolate synthetase; 1. DR Gene3D; 3.10.410.10; Formyltetrahydrofolate synthetase, domain 3; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_01543; FTHFS; 1. DR InterPro; IPR000559; Formate_THF_ligase. DR InterPro; IPR020628; Formate_THF_ligase_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01268; FTHFS; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00721; FTHFS_1; 1. DR PROSITE; PS00722; FTHFS_2; 1. PE 3: Inferred from homology; KW ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism; KW Reference proteome. FT CHAIN 1..551 FT /note="Formate--tetrahydrofolate ligase" FT /id="PRO_0000199354" FT BINDING 61..68 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543" SQ SEQUENCE 551 AA; 57936 MW; 6FA655CDF7526F7B CRC64; MKDIEIAQQV TPEPITAIAA KAGLTVDQID QYGSTKAKLK LPLPVKKTQR NLILVTSINP TPAGEGKSTV TIGLGDALTK IGKSTMIALR EPSLGPVMGM KGGATGGGYS QVIPMEDINL HFTGDMHALT AANNTLAALI DNHIQQGNQL GIDQRRIQWK RALDINDRAL RHTVIGLGGA TSGVPREDGF DITVASELMA ILCLSENIAD LKQRVNRIVI GYTHDRQPVT VADLNVGGAI TLLLKDALRP NLVQTLAHTP ALVHGGPFAN IAHGCNSVLA TQAGLNLADY TVTEAGFGAD LGGQKFMDIN VPAVGQAPNA VVIVATIRAL KLHGGVALQD LATENVAALK AGAANLGHHI HAMQRYGVPV VVAINEFTAD TDAEIHAVKD YCADLGVDAV LADVWGRGGD GATDLAAAVV DLCAQPSHFQ PLSPADADLK TKINDIVTKT YGGANVEYSA KAQRQLRTFA KQGWDHLPVC MAKTQYSLSD DPKRLGAPTG FTINVREFVP KLGAGFIVAL TGNVLTMPGL PKHPAALDMD ISDDGKISGL F //