ID FTHS_CLOBA Reviewed; 556 AA. AC B2UXU5; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 73. 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=CLH_0166; OS Clostridium botulinum (strain Alaska E43 / Type E3). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=508767; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Alaska E43 / Type E3; RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., RA Smith T.J., Sutton G., Brettin T.S.; RT "Complete genome sequence of Clostridium botulinum E3 str. Alaska E43."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. 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; CP001078; ACD51878.1; -; Genomic_DNA. DR RefSeq; WP_012450144.1; NC_010723.1. DR AlphaFoldDB; B2UXU5; -. DR SMR; B2UXU5; -. DR KEGG; cbt:CLH_0166; -. DR HOGENOM; CLU_003601_3_3_9; -. DR UniPathway; UPA00193; -. 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..556 FT /note="Formate--tetrahydrofolate ligase" FT /id="PRO_1000146676" FT BINDING 65..72 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543" SQ SEQUENCE 556 AA; 60263 MW; 89DA173F6453EE52 CRC64; MKTDIEIAQE AEMLHIRNIA EKLGLDEEDI EYYGKYKCKI SLDVYNKVKN NRDGKLVLVT AINPTPAGEG KSTVTVGLGD ALNKMGKNTV IALREPSLGP VFGIKGGAAG GGYAQVVPME DINLHFTGDM HAITSANNLL SAAIDNHIHQ GNNLRIDSRR IIFKRVMDMN DRALRKIIVG MGGKINGFVR EDGFTITVAS EIMAILCLAS DLEDLKHRMG DILIAYDLDG NPVYAKQLEI QGAMALLMKD AIKPNLVQTL ENTPALIHGG PFANIAHGCN SIMATKLSLK LGDIVVTEAG FGADLGAEKF FDIKCRYGNL KPCCVVIVAT IRALKHHGGV AKADLNIPNV EALRLGIANL EKQIENIKKF NVEPVVAINK FVSDSDEEVE FIKEFCEKLG VKVALSDVWA KGGDGGIELG EAVLDVIEKD KSSFKTLYKA DNTIEEKILT IAKEIYGADG VVYSNEAKKQ IGELVKFNLD KLPICMAKTQ YSLSDNPNLL AKPSGFNINV QEIRVSNGAG FIVVQTGNIM TMPGLPKVPA ANKMDVLKDG EIVGLF //