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   03-AUG-2022, entry version 89.
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; Firmicutes; 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 = (6S)-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:57454, ChEBI:CHEBI:456216; EC=6.3.4.3;
CC         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   PRIDE; Q1J4C0; -.
DR   EnsemblBacteria; ABF38816; ABF38816; MGAS10750_Spy1866.
DR   KEGG; spi:MGAS10750_Spy1866; -.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; TRQGFSK; -.
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; 3.40.50.300; -; 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; SSF52540; 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