ID   FTHS_BACFR              Reviewed;         555 AA.
AC   Q64U80;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 96.
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=BF2202;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD48949.1; -; Genomic_DNA.
DR   RefSeq; WP_005787533.1; NC_006347.1.
DR   RefSeq; YP_099483.1; NC_006347.1.
DR   AlphaFoldDB; Q64U80; -.
DR   SMR; Q64U80; -.
DR   STRING; 295405.BF2202; -.
DR   GeneID; 66328797; -.
DR   KEGG; bfr:BF2202; -.
DR   PATRIC; fig|295405.11.peg.2140; -.
DR   HOGENOM; CLU_003601_3_3_10; -.
DR   OrthoDB; 9761733at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000002197; 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..555
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_0000199333"
FT   BINDING         64..71
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   555 AA;  60418 MW;  E5497181B20F7530 CRC64;
     MKSDIEIARS VELKKIKQVA ESIGIPRDEV ENYGRYIAKI PEYLIDEEKV KKSNLILVTA
     ITATKAGIGK TTVSIGLALG LNKIGKKAIV ALREPSLGPC FGMKGGAAGG GYAQVLPMEK
     INLHFTGDFH AITSAHNMIS ALLDNYLYQN QSKGFGLKEI LWRRVLDVND RSLRNIVVGL
     GPKTNGITQE SGFDITPASE IMAILCLSKD VDDLRRRIEN ILLGYTYDNK PFTVKDLGVA
     GAITVLLKDA IHPNLVQTTE GTAAFVHGGP FANIAHGCNS ILATKMAMTF GDYVITEAGF
     GADLGAEKFY NIKCRKSGLQ PRLTVIVATA QGLKMHGGVS LDRIKEPNLE GLREGLRNLD
     KHVRNLHSFG QTVIVAFNKF ASDTDEEMEL LREHCEQLGV GYAINNAFSE GGEGAVDLAN
     LVVETIENKP SEPLQFTYND EDSVQQKIEK VATNLYGASV VTYSTLTRNK IKLIEEMGIG
     HYPVCIAKTQ YSFSADPKVY GAVDNFELHI KDIVINNGAE MIVAIAGEIM RMPGLPKEPQ
     ALHIDIVDGN IEGLS
//