FTHS_CLOBL
ID FTHS_CLOBL Reviewed; 557 AA.
AC A7GJB8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=CLI_3732;
OS Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Langeland / NCTC 10281 / Type F;
RA Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000728; ABS41963.1; -; Genomic_DNA.
DR RefSeq; WP_003399652.1; NC_009699.1.
DR AlphaFoldDB; A7GJB8; -.
DR SMR; A7GJB8; -.
DR EnsemblBacteria; ABS41963; ABS41963; CLI_3732.
DR KEGG; cbf:CLI_3732; -.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000002410; 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..557
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000318568"
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 557 AA; 60701 MW; 9A40CF97CAA27596 CRC64;
MFKSDIEIAQ ESKMKNIKNI AEKIGLTEED IDLYGKYKCK ISLDVLESNK DKKDGKLILV
TAINPTPAGE GKSTVTVGLG QALWKKNKKA VIALREPSLG PVFGIKGGAA GGGYSQVVPM
EDINLHFTGD MHAITSANNL LAAAIDNHIH QGNILKIDQR RILFKRVMDM NDRALRNVIV
ALGGKINGFP REDGFMITVA SEIMAILCLA EDLMDLKNKM GEILVAYSTE GKPIYCKDLE
VQGAMALLMK DAIKPNLVQT LENTPAIIHG GPFANIAHGC NSILGTKMAL KLGDYVITEA
GFGADLGAEK FFDIKCRKAN LKPNCVVIVA TVRALKYNGG IPKENLKEQN MEALSKGIKN
LGKHIENVNK FGVPAVVAIN KFISDTEEEI EFIKKYCKEL GAEVSIAEVW EKGGNGGLEL
ADKVLDTIEN KESKFNPIYE ETLNIKQKIE TIAQEIYGAE GVDYSKEAEK QISEIEKLDL
DKKPVCMAKT QYSLSDDAKL LGRPCGFRIN VKEVRISNGA GFIVVLTGNV MTMPGLPKKP
AANNMDVLSD GNIVGLF