FTHS_CLOBB
ID FTHS_CLOBB Reviewed; 556 AA.
AC B2TI29;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=CLL_A0173;
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B;
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-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; CP001056; ACD22749.1; -; Genomic_DNA.
DR RefSeq; WP_012423596.1; NC_018648.1.
DR AlphaFoldDB; B2TI29; -.
DR SMR; B2TI29; -.
DR EnsemblBacteria; ACD22749; ACD22749; CLL_A0173.
DR KEGG; cbk:CLL_A0173; -.
DR PATRIC; fig|935198.13.peg.157; -.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001195; 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..556
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_1000146677"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 556 AA; 60252 MW; 93134614A9466369 CRC64;
MKTDIEIAQE AEMLHIKNVA EKLGLDEENI EYYGKYKCKV SLDVYNKVKN NRDGKLVLVT
AINPTPAGEG KSTVTVGLGD ALNKMGKNTV IALREPSLGP VFGIKGGAAG GGYAQVVPME
DINLHFTGDM HAITSANNLL SAAIDNHIHQ GNNLRIDSRR IIFKRVMDMN DRALRKIIVG
MGGKINGFVR EDGFTITVAS EIMAILCLAS DLEDLKHRMG DILIAYDLDG NPVYAKQLEI
QGAMALLMKD AIKPNLVQTL ENTPALIHGG PFANIAHGCN SIMATKLSLK LGDIVVTEAG
FGADLGAEKF FDIKCRYGNL KPCCVVIVAT IRALKHHGGV AKADLNTPNV EALRLGIANL
EKQIENIKKF NVEPVVAINK FVSDSDEEVE FIKEFCEKLG VKVALSDVWA KGGDGGIELG
EAVLDVIEKD KSNFKTLYDT DKTIEEKILT IAKEIYGADG VVYSNEAKKQ IGELVKFNLD
KLPICMAKTQ YSLSDNPNLL AKPSGFNINV QEIRVSNGAG FIVVQTGNIM TMPGLPKVPA
ANKMDVLKDG EIVGLF