ID   FTHS1_STRPD             Reviewed;         556 AA.
AC   Q1JGN8;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Formate--tetrahydrofolate ligase 1 {ECO:0000255|HAMAP-Rule:MF_01543};
DE            EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE   AltName: Full=Formyltetrahydrofolate synthetase 1 {ECO:0000255|HAMAP-Rule:MF_01543};
DE            Short=FHS 1 {ECO:0000255|HAMAP-Rule:MF_01543};
DE            Short=FTHFS 1 {ECO:0000255|HAMAP-Rule:MF_01543};
GN   Name=fhs1 {ECO:0000255|HAMAP-Rule:MF_01543};
GN   OrderedLocusNames=MGAS10270_Spy1041;
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; ABF34106.1; -; Genomic_DNA.
DR   RefSeq; WP_002984561.1; NC_008022.1.
DR   AlphaFoldDB; Q1JGN8; -.
DR   SMR; Q1JGN8; -.
DR   EnsemblBacteria; ABF34106; ABF34106; MGAS10270_Spy1041.
DR   KEGG; sph:MGAS10270_Spy1041; -.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; CGEIMTM; -.
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..556
FT                   /note="Formate--tetrahydrofolate ligase 1"
FT                   /id="PRO_0000293063"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   556 AA;  59531 MW;  C0C6D133E3FD58E7 CRC64;
     MKSDIEIAQS VALQPITDIV KKVGIDGDDI ELYGKYKAKL SFEKMKAVEA NEPGKLLLVT
     AINPTPAGEG KSTMSIGLAD ALNQMGKKTM LALREPSLGP VMGIKGGAAG GGYAQVLPME
     DINLHFTGDM HAITTANNAL SALIDNHLQQ GNDLGIDPRR IIWKRVLDLN DRALRQVIVG
     LGSPVNGVPR EDGFDITVAS EIMAILCLAT DLKDLKKRLA DIVVAYTYDR KPVYVRDLKV
     EGALTLILKD AIKPNLVQTI YGTPALIHGG PFANIAHGCN SVLATSTALR LADYTVTEAG
     FGADLGAEKF LNIKVPNLPK APDAIVIVAT LRALKMHGGV AKSDLAAENC EAVRLGFANL
     KRHVENMRQF KVPVVVAINE FVADTEAEIA TLKALCEEIK VPVELASVWA NGAEGGLALA
     KTVVRVIDQE AADYKRLYSD EDTLEEKVIN IVTQIYGGKA VQFGPKAKTQ LKQFAEFGWD
     KLPVCMAKTQ YSFSDNPSLL GAPTDFDITI REFVPKTGAG FIVGLTGDVM TMPGLPKVPA
     AMAMDVAENG TALGLF