ID FTHS_STAAE Reviewed; 555 AA. AC A6QHR5; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, 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=NWMN_1625; OS Staphylococcus aureus (strain Newman). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=426430; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Newman; RX PubMed=17951380; DOI=10.1128/jb.01000-07; RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.; RT "Genome sequence of Staphylococcus aureus strain Newman and comparative RT analysis of staphylococcal genomes: polymorphism and evolution of two major RT pathogenicity islands."; RL J. Bacteriol. 190:300-310(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; AP009351; BAF67897.1; -; Genomic_DNA. DR RefSeq; WP_000149404.1; NZ_CP023390.1. DR AlphaFoldDB; A6QHR5; -. DR SMR; A6QHR5; -. DR KEGG; sae:NWMN_1625; -. DR HOGENOM; CLU_003601_3_3_9; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000006386; 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..555 FT /note="Formate--tetrahydrofolate ligase" FT /id="PRO_1000073557" FT BINDING 65..72 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543" SQ SEQUENCE 555 AA; 59884 MW; 75CAB62B84EB2A7D CRC64; MTHLSDLDIA NQSTLQPIKD IAASVGISED ALEPYGHYKA KIDINKITPR ENKGKVVLVT AMSPTPAGEG KSTVTVGLAD AFHELNKNVM VALREPALGP TFGIKGGATG GGYAQVLPME DINLHFNGDF HAITTANNAL SAFIDNHIHQ GNELGIDQRR IEWKRVLDMN DRALRHVNVG LGGPTNGVPR EDGFNITVAS EIMAILCLSR SIKDLKDKIS RITIGYTRDR KPVTVADLKV EGALAMILKD AIKPNLVQSI EGTPALVHGG PFANIAHGCN SILATETARD LADIVVTEAG FGSDLGAEKF MDIKVREAGF DPAAVVVVAT IRALKMHGGV AKDNLKEENV EAVKAGIVNL ERHVNNIKKF GVEPVVAINA FIHDTDAEVE YVKSWAKENN VRIALTEVWK KGGKGGVDLA NEVLEVIDQP NSFKPLYELE LPLEQKIEKI VTEIYGGSKV TFSSKAQKQL KQFKENGWDN YPVCMAKTQY SFSDDQTLLG APSGFEITIR ELEAKTGAGF IVALTGAIMT MPGLPKKPAA LNMDVTDDGH AIGLF //