FTHS_CLOBK
ID FTHS_CLOBK Reviewed; 557 AA.
AC B1IGY1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=CLD_0967;
OS Clostridium botulinum (strain Okra / Type B1).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okra / Type B1;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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; CP000939; ACA44058.1; -; Genomic_DNA.
DR RefSeq; WP_003399652.1; NC_010516.1.
DR AlphaFoldDB; B1IGY1; -.
DR SMR; B1IGY1; -.
DR EnsemblBacteria; ACA44058; ACA44058; CLD_0967.
DR KEGG; cbb:CLD_0967; -.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000008541; 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_1000146678"
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