ID FTHS_CLOBK Reviewed; 557 AA. AC B1IGY1; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 79. 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}; GN OrderedLocusNames=CLD_0967; OS Clostridium botulinum (strain Okra / Type B1). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=498213; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Okra / Type B1; RX PubMed=18060065; DOI=10.1371/journal.pone.0001271; RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.; RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within RT plasmids."; RL PLoS ONE 2:E1271-E1271(2007). 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; CP000939; ACA44058.1; -; Genomic_DNA. DR RefSeq; WP_003399652.1; NC_010516.1. DR AlphaFoldDB; B1IGY1; -. DR SMR; B1IGY1; -. DR KEGG; cbb:CLD_0967; -. DR HOGENOM; CLU_003601_3_3_9; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000008541; 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. FT CHAIN 1..557 FT /note="Formate--tetrahydrofolate ligase" FT /id="PRO_1000146678" FT BINDING 66..73 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543" SQ SEQUENCE 557 AA; 60701 MW; 9A40CF97CAA27596 CRC64; MFKSDIEIAQ ESKMKNIKNI AEKIGLTEED IDLYGKYKCK ISLDVLESNK DKKDGKLILV TAINPTPAGE GKSTVTVGLG QALWKKNKKA VIALREPSLG PVFGIKGGAA GGGYSQVVPM EDINLHFTGD MHAITSANNL LAAAIDNHIH QGNILKIDQR RILFKRVMDM NDRALRNVIV ALGGKINGFP REDGFMITVA SEIMAILCLA EDLMDLKNKM GEILVAYSTE GKPIYCKDLE VQGAMALLMK DAIKPNLVQT LENTPAIIHG GPFANIAHGC NSILGTKMAL KLGDYVITEA GFGADLGAEK FFDIKCRKAN LKPNCVVIVA TVRALKYNGG IPKENLKEQN MEALSKGIKN LGKHIENVNK FGVPAVVAIN KFISDTEEEI EFIKKYCKEL GAEVSIAEVW EKGGNGGLEL ADKVLDTIEN KESKFNPIYE ETLNIKQKIE TIAQEIYGAE GVDYSKEAEK QISEIEKLDL DKKPVCMAKT QYSLSDDAKL LGRPCGFRIN VKEVRISNGA GFIVVLTGNV MTMPGLPKKP AANNMDVLSD GNIVGLF //