FTHS_CLOBJ
ID FTHS_CLOBJ Reviewed; 557 AA.
AC C1FND0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=CLM_4009;
OS Clostridium botulinum (strain Kyoto / Type A2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kyoto / Type A2;
RA Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL Submitted (OCT-2008) 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}.
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DR EMBL; CP001581; ACO84041.1; -; Genomic_DNA.
DR RefSeq; WP_003359395.1; NC_012563.1.
DR AlphaFoldDB; C1FND0; -.
DR SMR; C1FND0; -.
DR STRING; 536232.CLM_4009; -.
DR EnsemblBacteria; ACO84041; ACO84041; CLM_4009.
DR KEGG; cby:CLM_4009; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001374; 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_1000185251"
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; 60708 MW; 7ACDF728FF10F3D3 CRC64;
MFKSDIEIAQ ESKMKNIKNI AEKIGLTEED IDLYGKYKCK ISLDVLKSNK DKKDGKLILV
TAINPTPAGE GKSTVTVGLG QALWKKNKKA VIALREPSLG PVFGIKGGAA GGGYSQVVPM
EDINLHFTGD MHAITSANNL LAAAIDNHIH QGNILKIDQR RILFKRVMDI NDRALRNVIV
ALGGKINGFP REDGFMITVA SEIMAILCLA EDLMNLKNKM 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 QYSLSDDARL LGRPCGFRIN VKEVRISNGA GFIVVLTGNV MTMPGLPKKP
AANNMNVLSD GNIVGLF