FTHS_CLOAB
ID FTHS_CLOAB Reviewed; 556 AA.
AC Q97EB3;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=CA_C3201;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK81137.1; -; Genomic_DNA.
DR PIR; F97293; F97293.
DR RefSeq; NP_349797.1; NC_003030.1.
DR RefSeq; WP_010966477.1; NC_003030.1.
DR AlphaFoldDB; Q97EB3; -.
DR SMR; Q97EB3; -.
DR STRING; 272562.CA_C3201; -.
DR PRIDE; Q97EB3; -.
DR EnsemblBacteria; AAK81137; AAK81137; CA_C3201.
DR GeneID; 44999694; -.
DR KEGG; cac:CA_C3201; -.
DR PATRIC; fig|272562.8.peg.3380; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000814; 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;
KW Reference proteome.
FT CHAIN 1..556
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000199337"
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; 60507 MW; 7B0629B679B832FE CRC64;
MKTDIEIAQE AKMEPIVKIA EKIGLNEDDI DLYGKYKCKI SLDVLKQNKN KQDGKLVLVT
AINPTPAGEG KSTVTVGLGE ALCKMNKNTV IALREPSLGP VFGIKGGAAG GGYAQVVPME
DINLHFTGDM HAITSANNLL CAAIDNHIHQ GNSLKIDQRR IVFKRVMDMN DRALRSIVVG
LGGKVNGFPR EDGFMITVAS EIMAILCLAN DLMDLKERMG KILIAYDLDG NPVYCRDLKV
EGAMAMLMKD AMKPNLVQTL ENTPAIIHGG PFANIAHGCN SILATKMALK LGDYVITEAG
FGADLGAEKF LDIKCRYGNL NPDCVVLVAT IRALKHHGGA LKEDLSKPNA KVLEKGLSNL
GKQIENIKKY GVPVVVAINK FITDSEEEIK CIEEYCSKQG VKVSLTEVWE KGGEGGTDLA
NKVLDTLENE KSNFKYLYDE KLSIKEKMDI IAKEIYGADG VQYTPQANKQ IKEIEKFNLD
KLPICVAKTQ YSLSDNPALL GRPTNFTINV KEVRVSNGAG FVVVQTGNIM TMPGLPKTPA
ANKMDIFEDG SIVGLF