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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
 
 
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