ID   FTHS2_STRPB             Reviewed;         557 AA.
AC   Q1J9F2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
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=MGAS2096_Spy1807;
OS   Streptococcus pyogenes serotype M12 (strain MGAS2096).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370553;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS2096;
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}.
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DR   EMBL; CP000261; ABF36859.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1J9F2; -.
DR   SMR; Q1J9F2; -.
DR   KEGG; spj:MGAS2096_Spy1807; -.
DR   HOGENOM; CLU_003601_3_3_9; -.
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; 3.30.1510.10; 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_0000293060"
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;  59054 MW;  448AACC11BDB9E2E CRC64;
     MVLSDIEIAN SVTMEPISKV ADQLGIDKEA LCLYGKYKAK IDARQLVALK NKPDGKLILV
     TAISPTPAGE GKTTTSVGLV DALSAIGKKA VIALREPSLG PVFGVKGGAA GGGHAQVVPM
     EDINLHFTGD FHAIGVANNL LAALIDNHIH HGNSLGIDSR RITWKRVVDM NDRQLRHIVD
     GLQGKVNGVP REDGYDITVA SEIMAILCLS ENISDLKAHL EKIIIGYNFQ GEPVTAKDLK
     AGGALAALLK DAIHPNLVQT LEHTPALIHG GPFANIAHGC NSVLATKLAL KYGDYAVTEA
     GFGADLGAEK FIDIKCRMSG LRPAAVVLVA TIRALKMHGG VPKADLATEN VQAVVDGLPN
     LDKHLANIQD VYGLPVVVAI NKFPLDTDAE LQAVYDACDK RGVDVVISDV WANGGAGGRE
     LAEKVVALAE QDNQFRFVYN EDDSIETKLT KIVTKVYGGK GIKLTPTAKR ELAELERLGF
     GNYPICMAKT QYSFSDDAKK LGAPTDFIVT ISNLKVSAGA GFIVALTGAI MTMPGLPKVP
     ASETIDIDEE GNITGLF
//