ID FTHS_STAAN Reviewed; 555 AA. AC Q7A535; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 05-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=SA1553; OS Staphylococcus aureus (strain N315). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=158879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N315; RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., RA Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus."; RL Lancet 357:1225-1240(2001). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=N315; RX PubMed=15590099; DOI=10.1016/j.mimet.2004.09.017; RA Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., RA Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., RA Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.; RT "Correlation of proteomic and transcriptomic profiles of Staphylococcus RT aureus during the post-exponential phase of growth."; RL J. Microbiol. Methods 60:247-257(2005). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=N315; RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.; RT "Shotgun proteomic analysis of total and membrane protein extracts of S. RT aureus strain N315."; RL Submitted (OCT-2007) to UniProtKB. 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; BA000018; BAB42821.1; -; Genomic_DNA. DR PIR; H89957; H89957. DR RefSeq; WP_000149407.1; NC_002745.2. DR AlphaFoldDB; Q7A535; -. DR SMR; Q7A535; -. DR EnsemblBacteria; BAB42821; BAB42821; BAB42821. DR KEGG; sau:SA1553; -. DR HOGENOM; CLU_003601_3_3_9; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000000751; 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. DR SWISS-2DPAGE; Q7A535; -. PE 1: Evidence at protein level; KW ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism. FT CHAIN 1..555 FT /note="Formate--tetrahydrofolate ligase" FT /id="PRO_0000199380" 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; 59872 MW; E71E884FF0368174 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 DLAAVVVVAT IRALKMHGGV AKDNLKEENV EAVKAGIVNL ERHVNNIKKF GVEPVVAINA FIHDTDAEVE YVKSWAKENN VRIALTEVWE KGGKGGVDLA NEVLEVIDQP NSFKPLYELE LPLEQKIEKI VTEIYGGSKV TFSSKAQKQL KQFKENGWDN YPVCMAKTQY SFSDDQTLLG APSGFEITIR ELEAKTGAGF IVALTGAIMT MPGLPKKPAA LNMDVTDDGH AIGLF //