ID   FTHS2_STRPQ             Reviewed;         557 AA.
AC   P0DF93; Q79W25; Q8K5L8;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 57.
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}; Synonyms=fhs.2;
GN   OrderedLocusNames=SPs1773;
OS   Streptococcus pyogenes serotype M3 (strain SSI-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=193567;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSI-1;
RX   PubMed=12799345; DOI=10.1101/gr.1096703;
RA   Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA   Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA   Hattori M., Hamada S.;
RT   "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT   scale genomic rearrangement in invasive strains and new insights into phage
RT   evolution.";
RL   Genome Res. 13:1042-1055(2003).
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; BA000034; BAC64868.1; -; Genomic_DNA.
DR   RefSeq; WP_011055075.1; NC_004606.1.
DR   AlphaFoldDB; P0DF93; -.
DR   SMR; P0DF93; -.
DR   GeneID; 57853439; -.
DR   KEGG; sps:SPs1773; -.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; TRQGFSK; -.
DR   UniPathway; UPA00193; -.
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_0000411586"
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;  59052 MW;  029820DF95BB401A CRC64;
     MVLSDIEIAN SVTMEPISKV ANQLGIDEEA LCLYGKYKAK IDARQLVALK DKPDGKLILV
     TAISPTPAGE GKTTTSVGLV DALSAIGKKA VIALREPSLG PVFGVKGGAA GGGHAQVVPM
     EDINLHFTGD FHAIGVANNL LAALIDNHIH HGNSLGIDSR RITWKRVVDM NDRQLRHIVD
     GLQGKVNGAP REDGYDITVA SEIMAILCLS ENISDLKARL EKIIIGYNYR GEPVTAKDLK
     AGGALAALLK DAIHPNLVQT LEHTPALIHG GPFANIAHGC NSVLATKLAL KYGDYAVTEA
     GFGADLGAEK FIDIKCRMSG LRPAAVVLVA TIRALKMHGG VPKADLATEN VQAVVDGLPN
     LDKHLANIQD VYGLPVVVAI NKFPLDTDAE LQAVYDACDK RGVDVVISDV WANGGAGARE
     LAEKVVTLAE QDNQFRFVYE EDDSIETKLT KIVTKVYGGK GITLSPAAKR ELADLERLGF
     GNYPICMAKT QYSFSDDAKK LGAPTDFTVT ISNLKVSAGA GFIVALTGAI MTMPGLPKVP
     ASETIDIDEE GNITGLF