ID FTHS_NEIM0 Reviewed; 558 AA. AC A9M1J1; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 84. 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=NMCC_0383; OS Neisseria meningitidis serogroup C (strain 053442). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=374833; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=053442; RX PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004; RA Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z., RA Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z., RA Liang X., Xu J., Jin Q.; RT "Characterization of ST-4821 complex, a unique Neisseria meningitidis RT clone."; RL Genomics 91:78-87(2008). 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; CP000381; ABX72589.1; -; Genomic_DNA. DR RefSeq; WP_012221285.1; NC_010120.1. DR AlphaFoldDB; A9M1J1; -. DR SMR; A9M1J1; -. DR KEGG; nmn:NMCC_0383; -. DR HOGENOM; CLU_003601_3_3_4; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000001177; 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..558 FT /note="Formate--tetrahydrofolate ligase" FT /id="PRO_1000087652" FT BINDING 66..73 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543" SQ SEQUENCE 558 AA; 59103 MW; 296C2FC7EC4FEFD3 CRC64; MSFKTDAEIA QSSTMRPIGE IAAKLGLNAD NIEPYGHYKA KINPAEAFKL PQKQGRLILV TAINPTPAGE GKTTVTIGLA DALRHIGKDS VIALREPSLG PVFGVKGGAA GGGYAQVLPM EDINLHFTGD FHAIGAANNL LAAMLDNHIY QGNELDIDPK RVLWRRVVDM NDRQLRNIID GMGKPVDGVM RPDGFDITVA SEVMAVFCLA KDISDLKERL GNILVAYAKD GSPVYAKDLK ANGAMAALLK DAIKPNLVQT IEGTPAFVHG GPFANIAHGC NSVTATRLAK HLADYAVTEA GFGADLGAEK FCDIKCRLAG LKPDAAVVVA TVRALKYNGG VERANLGEEN LDALEKGLPN LLKHISNLKN VFGLPVVVAL NRFVSDSDAE LAMIEKACAE HGVEVSLTEV WGKGGAGGAD LARKVVNAIE SQTNNFGFAY DVELGIKDKI RAIAQKVYGA EDVDFSAEAS AEIASLEKLG LDKMPICMAK TQYSLSDNAK LLGCPEGFRI AVRGITVSAG AGFIVALCGN MMKMPGLPKV PAAEKIDVDE HGVIHGLF //