ID   FTHS_BACC1              Reviewed;         562 AA.
AC   Q739F4;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=BCE_2187;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
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; AE017194; AAS41108.1; -; Genomic_DNA.
DR   RefSeq; WP_011040261.1; NC_003909.8.
DR   AlphaFoldDB; Q739F4; -.
DR   SMR; Q739F4; -.
DR   EnsemblBacteria; AAS41108; AAS41108; BCE_2187.
DR   KEGG; bca:BCE_2187; -.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; CGEIMTM; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000002527; 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..562
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_0000199328"
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;  60448 MW;  263018CC73746E69 CRC64;
     MTTTTTVKSD IEIAQEASMK 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
     EGEGWSNLPV CMAKTQYSLS DDATKLGRPS DFIVTIRELK PSIGAGFIVA LTGTMLTMPG
     LPKQPAALQM DVNEDGKAVG LF