ID   A7GP45_BACCN            Unreviewed;       583 AA.
AC   A7GP45;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   02-SEP-2026, entry version 116.
DE   RecName: Full=Formate--tetrahydrofolate ligase {ECO:0000256|HAMAP-Rule:MF_01543};
DE            EC=6.3.4.3 {ECO:0000256|HAMAP-Rule:MF_01543};
DE   AltName: Full=Formyltetrahydrofolate synthetase {ECO:0000256|HAMAP-Rule:MF_01543};
DE            Short=FHS {ECO:0000256|HAMAP-Rule:MF_01543};
DE            Short=FTHFS {ECO:0000256|HAMAP-Rule:MF_01543};
GN   Name=fhs {ECO:0000256|HAMAP-Rule:MF_01543};
GN   OrderedLocusNames=Bcer98_1593 {ECO:0000313|EMBL:ABS21903.1};
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus; Bacillus cereus group.
OX   NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS21903.1, ECO:0000313|Proteomes:UP000002300};
RN   [1] {ECO:0000313|EMBL:ABS21903.1, ECO:0000313|Proteomes:UP000002300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC   {ECO:0000313|Proteomes:UP000002300};
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.H., Sanchis V.,
RA   Nguen-The C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + formate + ATP = (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:0000256|ARBA:ARBA00049033,
CC         ECO:0000256|HAMAP-Rule:MF_01543};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|HAMAP-Rule:MF_01543}.
CC   -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.
CC       {ECO:0000256|ARBA:ARBA00061363, ECO:0000256|HAMAP-Rule:MF_01543}.
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DR   EMBL; CP000764; ABS21903.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7GP45; -.
DR   STRING; 315749.Bcer98_1593; -.
DR   PaxDb; 315749-Bcer98_1593; -.
DR   KEGG; bcy:Bcer98_1593; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000002300; 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-UniRule.
DR   CDD; cd00477; FTHFS; 1.
DR   FunFam; 3.30.1510.10:FF:000001; Formate--tetrahydrofolate ligase; 1.
DR   FunFam; 3.10.410.10:FF:000001; Putative formate--tetrahydrofolate ligase; 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   NCBIfam; NF010030; PRK13505.1; 1.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01543};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01543};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01543};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW   Rule:MF_01543}; Reference proteome {ECO:0000313|Proteomes:UP000002300}.
FT   BINDING         92..99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   583 AA;  62903 MW;  2AB4C4A5DB515671 CRC64;
     MQKIQKTDTI WSEPIKGGLG YMTTTTTVKS DIEIAQEARM KKIQDIAAEL DILEEELEPY
     GHYKGKLSLD IFKRLQTKTE GKVVLVTAIN PTPAGEGKST VTVGLGQAFH KIGKKAVIAL
     REPSLGPTMG LKGGAAGGGY SQVVPMEDIN LHFTGDIHAI TTANNALAAF IDNHIQQGNA
     LQIDTRKIVW KRCVDLNDRA LRNVVIGLGG PVQGVPREDG FDITVASEIM AVFCLATDIQ
     DLKARLSRIV VAYNFENQPV TVKDLGVEGA LTLLLKDALK PNLVQTLENT PAIIHGGPFA
     NIAHGCNSVI ATTMAAKLGD YVITEAGFGA DLGAEKFLDI KARAAGIKPE AVVIVATIRA
     LKMHGGVAKD QLKEENVDAL AKGMENLQKH VETIQSFGVP FVIAINKFIT DTDAEVAYLQ
     KWCNERGYEV SLTEVWEKGG QGGVDLAEKV LKVIEKGENK YAPLYDLNAS LEEKIRTIAQ
     KVYGAKDIEF APKARKQLAQ FEGEGWGNLP VCMAKTQYSL SDDATKLGRP SDFIVTIREL
     KPSIGAGFIV ALTGTMLTMP GLPKQPAALQ MDVNEDGKAV GLF
//