FTHS_CLOTE
ID FTHS_CLOTE Reviewed; 559 AA.
AC Q891R3;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=CTC_02304;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO36782.1; -; Genomic_DNA.
DR RefSeq; WP_011100443.1; NC_004557.1.
DR AlphaFoldDB; Q891R3; -.
DR SMR; Q891R3; -.
DR STRING; 212717.CTC_02304; -.
DR EnsemblBacteria; AAO36782; AAO36782; CTC_02304.
DR GeneID; 64179618; -.
DR KEGG; ctc:CTC_02304; -.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; TRQGFSK; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001412; 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..559
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000199341"
FT BINDING 68..75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 559 AA; 60073 MW; 5FF7F0F0943AF04B CRC64;
MEKVLTDIEI AQKAQMKPIG EIAEKYGILE DELELYGKYK AKLSLDIFDR LKDEKDGKLV
LVTAISPTPA GEGKSTTSIG LGQALNKIGK KTFIALREPS LGPVFGVKGG AAGGGYAQVV
PMEDINLHFT GDMHAIGITN NLLSAAIDNH IHQGNALKID SREIVWKRVV DMNDRALRNV
VVGMGGKACG FTRQDGFMIT VASEVMAILC LAKDLMDLKE RLGNIIVAYS LEGKPVTAGD
LKVNGAMAML LKDAIKPNIV QTLENTPALI HGGPFANIAH GCNSLIATRL GLKLGDILVT
EAGFGADLGA EKFLDIKCRY GGLKPDAVVI VATIRALKMH GGVKKTELSG ENLEALDKGF
ANLQKHITNM KNFGLPVMVA VNRFITDSEA EIDLLIKKCK EIGVEVSLNE VWAKGGEGGI
EMAEKLVKIL ETEKPNYKPL YDVEDSIPEK LNKIVKELYG GEGVVIESSA MKQIKKLEEI
GLDKLPICMA KTQFSFSDDA TLMGAPKGFN ITIKNVRVSA GAGFIVCETG NIMVMPGLPK
VPAAEKMDVD ENGNISGLF