ID   FTHS_CLOK5              Reviewed;         558 AA.
AC   A5N5B3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
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=CKL_0440;
OS   Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=431943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680;
RX   PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA   Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA   Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA   Hagemeier C., Thauer R.K., Gottschalk G.;
RT   "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT   metabolic features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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; CP000673; EDK32494.1; -; Genomic_DNA.
DR   RefSeq; WP_011989009.1; NC_009706.1.
DR   AlphaFoldDB; A5N5B3; -.
DR   SMR; A5N5B3; -.
DR   STRING; 431943.CKL_0440; -.
DR   KEGG; ckl:CKL_0440; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000002411; 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;
KW   Reference proteome.
FT   CHAIN           1..558
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_1000087651"
FT   BINDING         66..73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   558 AA;  60414 MW;  6E7ABE3A88C40AE8 CRC64;
     MNFKSDIQIA QECSMENIKD IAKKLNIFED EIELYGKYKA KIDYNLLKTT KGKNGKLILC
     TAINPTPAGE GKTTTSIGVA DALARLDKSV VVALREPSMG PVFGIKGGAA GGGYAQVVPM
     EDINLHFTGD IHAMTAANNL LAALIDNHIY QGNKLNIDSR RVVWRRCVDM NDRQLRFVVD
     GLGGKVNGIP REDGFDITVA SEIMAIFCLS TDINDLKERI SKIVVGYTTE GNPVTAHDLK
     AEGAMAALLK DALKPNLVQT LEGTPAFVHG GPFANIAHGC NSIMATRMAM HFGDYVVTEA
     GFGADLGAEK FLDIKCRMAG LRPDAVIIVA TVRALKYNGG TPKTKLNNEN LETLEKGIPN
     LLKHVENITK VFKLPAVVAL NAFPTDTEAE LKLVEEKCRE FGVSVKLSEV WAKGGEGGIE
     VAKEVLRLIN EGKNDFQFAY DEKLPIRDKI RAIAQKIYGA DGVTFTNQAE KEIDELEKLG
     FGKTPVCIAK TQYSLTDDQN KLGRPKGFKI TVRQVSISAG AGFVVAITGS IMKMPGLPKV
     PAAEKIDVDE NGVISGLF
//