ID FTHS_STRA3 Reviewed; 556 AA. AC Q8E5E3; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 103. 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=gbs1089; OS Streptococcus agalactiae serotype III (strain NEM316). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=211110; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NEM316; RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x; RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T., RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.; RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive RT neonatal disease."; RL Mol. Microbiol. 45:1499-1513(2002). 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; AL766848; CAD46748.1; -; Genomic_DNA. DR RefSeq; WP_000845316.1; NC_004368.1. DR AlphaFoldDB; Q8E5E3; -. DR SMR; Q8E5E3; -. DR KEGG; san:gbs1089; -. DR eggNOG; COG2759; Bacteria. DR HOGENOM; CLU_003601_3_3_9; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000000823; 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..556 FT /note="Formate--tetrahydrofolate ligase" FT /id="PRO_0000199384" 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; 59933 MW; 562ECB49DF82D336 CRC64; MKTDIEIAQS VALKPIAEIV EQVGIGFDDI ELYGKYKAKL SFDKIEAVRS QKVGKLILVT AINPTPAGEG KSTMSIGLAD ALNKIGKKTM IALREPSLGP VMGIKGGAAG GGYAQVLPME DINLHFTGDM HAITTANNAL SALLDNHIHQ GNELDIDQRR VIWKRVVDLN DRALRQVIVG LGSSVNGIPR EDGFDITVAS EIMAILCLAT DLSDLKKRLS NIVVAYSRDR KPIYVKDLKI EGALTLILKD AIKPNLVQTI YGTPALVHGG PFANIAHGCN SVLATSTALR LADYVVTEAG FGADLGAEKF LDIKTPNLPT SPDAIVIVAT LRALKMHGGV SKEDLSQENV KAVKRGFTNL ERHVNNMRQY GVPVVVAINQ FTADTESEIA TLKTLCSNID VAVELASVWE DGADGGLELA QTVANVIETQ SSNYKRLYND EDTIEEKIKK IVTKIYGGNK VHFGPKAQIQ LKEFSDNGWD KMPICMAKTQ YSFSDNPNLL GAPTDFDITV REFVPKTGAG FIVALTGDVL TMPGLPKKPA ALNMDVLEDG TAIGLF //