ID   FTHS_CLOBA              Reviewed;         556 AA.
AC   B2UXU5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=CLH_0166;
OS   Clostridium botulinum (strain Alaska E43 / Type E3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=508767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alaska E43 / Type E3;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete genome sequence of Clostridium botulinum E3 str. Alaska E43.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001078; ACD51878.1; -; Genomic_DNA.
DR   RefSeq; WP_012450144.1; NC_010723.1.
DR   AlphaFoldDB; B2UXU5; -.
DR   SMR; B2UXU5; -.
DR   KEGG; cbt:CLH_0166; -.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; CGEIMTM; -.
DR   OrthoDB; 177859at2; -.
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"
FT                   /id="PRO_1000146676"
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;  60263 MW;  89DA173F6453EE52 CRC64;
     MKTDIEIAQE AEMLHIRNIA EKLGLDEEDI EYYGKYKCKI SLDVYNKVKN NRDGKLVLVT
     AINPTPAGEG KSTVTVGLGD ALNKMGKNTV IALREPSLGP VFGIKGGAAG GGYAQVVPME
     DINLHFTGDM HAITSANNLL SAAIDNHIHQ GNNLRIDSRR IIFKRVMDMN DRALRKIIVG
     MGGKINGFVR EDGFTITVAS EIMAILCLAS DLEDLKHRMG DILIAYDLDG NPVYAKQLEI
     QGAMALLMKD AIKPNLVQTL ENTPALIHGG PFANIAHGCN SIMATKLSLK LGDIVVTEAG
     FGADLGAEKF FDIKCRYGNL KPCCVVIVAT IRALKHHGGV AKADLNIPNV EALRLGIANL
     EKQIENIKKF NVEPVVAINK FVSDSDEEVE FIKEFCEKLG VKVALSDVWA KGGDGGIELG
     EAVLDVIEKD KSSFKTLYKA DNTIEEKILT IAKEIYGADG VVYSNEAKKQ IGELVKFNLD
     KLPICMAKTQ YSLSDNPNLL AKPSGFNINV QEIRVSNGAG FIVVQTGNIM TMPGLPKVPA
     ANKMDVLKDG EIVGLF