ID   FTHS1_STRPQ             Reviewed;         556 AA.
AC   P0DF91; Q79X48; Q7CF36;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 52.
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}; Synonyms=fhs;
GN   OrderedLocusNames=SPs1053;
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; BAC64148.1; -; Genomic_DNA.
DR   RefSeq; WP_002989724.1; NC_004606.1.
DR   AlphaFoldDB; P0DF91; -.
DR   SMR; P0DF91; -.
DR   KEGG; sps:SPs1053; -.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; CGEIMTM; -.
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..556
FT                   /note="Formate--tetrahydrofolate ligase 1"
FT                   /id="PRO_0000411585"
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;  90C6D132DF20EE3C CRC64;
     MKSDIEIAQS VALQPITDIV KKVGIDGDDI ELYGKYKAKL SFEKMKAVEA NEPGKLILVT
     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