ID   FTHS_STREM              Reviewed;         556 AA.
AC   B4U2T6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Formate--tetrahydrofolate ligase {ECO:0000255|HAMAP-Rule:MF_01543};
DE            EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE   AltName: Full=Formyltetrahydrofolate synthetase {ECO:0000255|HAMAP-Rule:MF_01543};
DE            Short=FHS {ECO:0000255|HAMAP-Rule:MF_01543};
DE            Short=FTHFS {ECO:0000255|HAMAP-Rule:MF_01543};
GN   Name=fhs {ECO:0000255|HAMAP-Rule:MF_01543}; OrderedLocusNames=Sez_0945;
OS   Streptococcus equi subsp. zooepidemicus (strain MGCS10565).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=552526;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGCS10565;
RX   PubMed=18716664; DOI=10.1371/journal.pone.0003026;
RA   Beres S.B., Sesso R., Pinto S.W.L., Hoe N.P., Porcella S.F., Deleo F.R.,
RA   Musser J.M.;
RT   "Genome sequence of a lancefield group C Streptococcus zooepidemicus strain
RT   causing epidemic nephritis: new information about an old disease.";
RL   PLoS ONE 3:E3026-E3026(2008).
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; CP001129; ACG62303.1; -; Genomic_DNA.
DR   RefSeq; WP_012515574.1; NC_011134.1.
DR   AlphaFoldDB; B4U2T6; -.
DR   SMR; B4U2T6; -.
DR   EnsemblBacteria; ACG62303; ACG62303; Sez_0945.
DR   KEGG; sez:Sez_0945; -.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; CGEIMTM; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000001873; 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"
FT                   /id="PRO_1000196825"
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;  59434 MW;  6EEE31A9E5D71EB5 CRC64;
     MKSDIEIAQS VPLKPITEIV KKVGIDGDDL ELYGNYKAKL SFEKIKSVKG NKPGKLILVT
     AINPTPAGEG KSTMSIGLAD ALTKIGKKTM LALREPSLGP VMGIKGGAAG GGYAQVLPME
     DINLHFTGDM HAITTAHNAL SALIDNHLQQ GNELGIDPRR IIWKRVLDLN DRSLRQVIVG
     LGSPVNGVPR EDGFDITVAS EVMAILCLAT DLKDLKARLA NIVIAYRYDK SPVYVRDLKV
     EGALALILKD AIKPNLVQTI YGTPAFVHGG PFANIAHGCN SVLATSTALR LADYTVTEAG
     FGADLGAEKF LNIKTPNLPK APDAVVIVAT LRALKMHGGV AKADLTFENT AAVRSGFANL
     KRHVENIRKF NIPVVVAINE FVTDTKAEIQ VLKELCAEIA VPVELASVWA KGADGGIALA
     NAVVSAIAEE SAAYKRLYAD KDSLEEKLRA IVTEIYGGRT VQFGPKAKNQ LKQFAQYGWD
     QLPVCMAKTQ YSFSDDPSLL GAPDQFDITI RELVPKTGAG FIVALTGDVM TMPGLPKIPA
     AMKMDVTEDG TAVGLF