ID FTHS_STRS2 Reviewed; 556 AA. AC A4W0G0; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 80. 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=SSU98_0691; OS Streptococcus suis (strain 98HAH33). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=391296; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=98HAH33; RX PubMed=17375201; DOI=10.1371/journal.pone.0000315; RA Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X., RA Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J., RA Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F., RA Yang R., Wang J., Yu J.; RT "A glimpse of streptococcal toxic shock syndrome from comparative genomics RT of S. suis 2 Chinese isolates."; RL PLoS ONE 2:E315-E315(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; CP000408; ABP91849.1; -; Genomic_DNA. DR AlphaFoldDB; A4W0G0; -. DR SMR; A4W0G0; -. DR KEGG; ssv:SSU98_0691; -. 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_0000300549" 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; 59108 MW; 6CC2ED05FD864616 CRC64; MKTDIDIAQS ITLKPITEIV EKVGISFDDI ELYGKYKAKL SFDKINAVKD NAPGKLILVT AINPTPAGEG KSTITIGLAD ALSKIGKKTM IALREPSLGP VMGIKGGAAG GGYAQVLPME DINLHFTGDM HAITTANNAL SALIDNHIHQ GNVIGIDQRR IIWKRVVDLN DRALRKVTVG LGGPLNGIPR EDGFDITVAS EIMAILCLAT DINDLKERLA NIVIGYRFDC SPVYVRDLAV EGALTLILKD AIKPNLVQTI YGTPAFVHGG PFANIAHGCN SVLATTTALR LADYTVTEAG FGADLGAEKF LDIKVPNLPK APDAVVIVAT LRALKMHGGV AKTELSAENV EAVKAGFSNL KRHVENIRKY GIPAVVAINE FVSDTAAEIA VLKELCAAIG VPVELASVWA NGADGGVELA ETVVATIDNQ AASYQRLYKS EDSLEEKVTK IVTQIYGGTG VVFEKKARNQ LTEFAKNGWD KLPVCMAKTQ YSFSDDQFAL GAPTDFDITV REFVPKLGAG FIVALTGDVM TMPGLPKAPV ALNMDVAADG TAIGLF //