ID   FTHS2_STRPD             Reviewed;         557 AA.
AC   Q1JEK4;
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=MGAS10270_Spy1840;
OS   Streptococcus pyogenes serotype M2 (strain MGAS10270).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370552;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS10270;
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}.
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DR   EMBL; CP000260; ABF34905.1; -; Genomic_DNA.
DR   RefSeq; WP_020905559.1; NC_008022.1.
DR   AlphaFoldDB; Q1JEK4; -.
DR   SMR; Q1JEK4; -.
DR   EnsemblBacteria; ABF34905; ABF34905; MGAS10270_Spy1840.
DR   KEGG; sph:MGAS10270_Spy1840; -.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; TRQGFSK; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000002436; 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_0000293064"
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;  59066 MW;  4DFEB9DD8F5B11C7 CRC64;
     MVLSDIEIAN SVSMEPISKV ADQLGIDKEA LCLYGKYKAK INARQLVALK DKPDGKLILV
     TTISPTPAGE GKTTTSVGLV DALSAIGKKA VIALREPSLG PVFGVKGGAA GGGHAQVVPM
     EDINLHFTGD FHAIGVANNL LAALIDNHIH HGNSLGIDSR RITWKRVVDM NDRQLRHIVD
     GLQGKVNGVP REDGYDITVA SEIMAILCLS ENISDLKARL EKIIIGYNYQ GEPVTAKDLK
     AGGALAALLK DAIHPNLVQT LEHTPALIHG GPFANIAHGC NSVLATKLAL KYGDYAVTEA
     GFGADLGAEK FIDIKCRMSG LRPAAVVLVA TIRALKMHGG VPKADLATEN VQAVVDGLPN
     LDKHLANIQD VYGLPVVVAI NKFPLDTDAE LQAVYDACNK RGVDVVISDV WANGGAGGRE
     LAEKVVTLAE QDNQFRFVYE EDDSIETKLT KIVTKVYGGK GITLTPAAKR ELADLERLGF
     GNYPICMAKT QYSFSDDAKK LGAPTDFTVT ISNLKVSAGA GFIVALTGAI MTMPGLPKVP
     ASETIDIDEE GNITGLF