ID FTHS2_STRPF Reviewed; 557 AA. AC Q1J4C0; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 1. DT 27-MAR-2024, entry version 96. DE RecName: Full=Formate--tetrahydrofolate ligase 2 {ECO:0000255|HAMAP-Rule:MF_01543}; DE EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543}; DE AltName: Full=Formyltetrahydrofolate synthetase 2 {ECO:0000255|HAMAP-Rule:MF_01543}; DE Short=FHS 2 {ECO:0000255|HAMAP-Rule:MF_01543}; DE Short=FTHFS 2 {ECO:0000255|HAMAP-Rule:MF_01543}; GN Name=fhs2 {ECO:0000255|HAMAP-Rule:MF_01543}; GN OrderedLocusNames=MGAS10750_Spy1866; OS Streptococcus pyogenes serotype M4 (strain MGAS10750). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=370554; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGAS10750; RX PubMed=16636287; DOI=10.1073/pnas.0510279103; RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R., RA Musser J.M.; RT "Molecular genetic anatomy of inter- and intraserotype variation in the RT human bacterial pathogen group A Streptococcus."; RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006). 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; CP000262; ABF38816.1; -; Genomic_DNA. DR RefSeq; WP_011529082.1; NC_008024.1. DR AlphaFoldDB; Q1J4C0; -. DR SMR; Q1J4C0; -. DR KEGG; spi:MGAS10750_Spy1866; -. DR HOGENOM; CLU_003601_3_3_9; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000002434; 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..557 FT /note="Formate--tetrahydrofolate ligase 2" FT /id="PRO_0000293066" FT BINDING 66..73 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543" SQ SEQUENCE 557 AA; 59100 MW; DC64485B7C6E612B CRC64; MVLSDIEIAN SVSMEPISKV ADQLGIDKEA LCLYGKYKAK INARQLVALK DKPDGKLILV TAISPTPAGE GKTTTSVGLV DALSAIGKKA VIALREPSLG PVFGVKGGAA GGGHAQVVPM EDINLHFTGD FHAIGVANNL LAALIDNHIH HGNSLGIDSR RITWKRVVDM NDRQLRHIVD GLQGKVNGVP REDGYDITVA SEIMAILCLS ENISDLKARL EKIIIGYNYQ GEPVTAKDLK AGGALADLLK DAIHPNLVQT LEHTPALIHG GPFANIAHGC NSVLATKLAL KYGDYAVTEA GFGADLGAEK FIDIKCRMSG LRPAAVVLVA TIRALKMHGG VQKTDLATEN VQAVVDGLPN LDKHLANIQD VYGLPVVVAI NKFPLDTDAE LQAVYDACNK RGVDVVISDV WANGGAGGRE LAEKVVTLAE QDNQFRFVYE EDDSIETKLT KIVTKVYGGK GITLSPAAKR ELADLERLGF GNYPICMAKT QYSFSDDAKT LGAPTDFTVT ISNLKVSAGA GFIVALTGAI MTMPGLPKVP ASETIDIDEE GNITGLF //