ID   FTHS_BACC0              Reviewed;         562 AA.
AC   B7JLG8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
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};
GN   OrderedLocusNames=BCAH820_2141;
OS   Bacillus cereus (strain AH820).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405535;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH820;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH820.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001283; ACK91551.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7JLG8; -.
DR   SMR; B7JLG8; -.
DR   KEGG; bcu:BCAH820_2141; -.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000001363; 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; 3.30.1510.10; 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..562
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_1000146672"
FT   BINDING         71..78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   562 AA;  60489 MW;  39136D9134276E69 CRC64;
     MTTTTTVKSD IEIAQEANMK KIQEIAADLN ILEDELEPYG HYKGKLSLDI FKRLQNEKDG
     KVVLVTAINP TPAGEGKSTV TVGLGQAFNK IGKKTVIALR EPSLGPTMGL KGGAAGGGFS
     QVVPMEDINL HFTGDIHAIT TANNALAAFI DNHIQQGNTL GIDTRKIVWK RCVDLNDRAL
     RNVVIGLGGP VQGVPREDGF DITVASEIMA VFCLATDIQD LKARLSRIVV AYNFANQPVT
     VKDLGVEGAL TLLLKDALKP NLVQTLENTP AIIHGGPFAN IAHGCNSVIA TTMAAKLGDY
     VITEAGFGAD LGAEKFLDIK ARAAGIKPEA VVIVATIRAL KMHGGVAKDQ LKEENVDALA
     KGMENLQKHV ETIQSFGVPF VIAINKFITD TDAEVAYLQE WCNERGYAVS LTEVWEKGGQ
     GGVDLAEKVL KEIEKGENNY APLYELELPL EEKIRTIAQK VYGAKDIEFA PKARKQLAQY
     EGEGWSNLPI CMAKTQYSLS DDATKLGRPS DFIVTIRELK PSIGAGFIVA LTGTMLTMPG
     LPKQPAALQM DVNEDGKAVG LF
//