ID FTHS_STAAR Reviewed; 555 AA. AC Q6GFX6; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 100. 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}; OrderedLocusNames=SAR1810; OS Staphylococcus aureus (strain MRSA252). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=282458; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MRSA252; RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence RT for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004). 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; BX571856; CAG40801.1; -; Genomic_DNA. DR RefSeq; WP_000149412.1; NC_002952.2. DR AlphaFoldDB; Q6GFX6; -. DR SMR; Q6GFX6; -. DR KEGG; sar:SAR1810; -. DR HOGENOM; CLU_003601_3_3_9; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000000596; 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_0000199376" 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; 59856 MW; 371849E3EAF8B997 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 QGALAMILKD AIKPNLVQSI EGTPALVHGG PFANIAHGCN SILATETARD LADIVVTEAG FGSDLGAEKF MDIKAREAGF DPAAVVVVAT IRALKMHGGV AKDNLKEENV EAVKAGIVNL ERHVNNIKKF GVEPVVAINA FIHDTDAEVE YVKSWAKENN VRIALTEVWE KGGKGGVDLA NEVLEVIDQP NSFKPLYELE LPLEQKIEKI VTEIYGGSKV TFSSKAQKQL KQFKENGWDN YPVCMAKTQY SFSDDQTLLG APSGFEITIR ELEAKTGAGF IVALTGAIMT MPGLPKKPAA LNMDVTDDGH AIGLF //