ID   FTHS_THEAB              Reviewed;         551 AA.
AC   B7IG29;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=THA_555;
OS   Thermosipho africanus (strain TCF52B).
OC   Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX   NCBI_TaxID=484019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCF52B;
RX   PubMed=19124572; DOI=10.1128/jb.01448-08;
RA   Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA   Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT   "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT   the Firmicutes and Archaea.";
RL   J. Bacteriol. 191:1974-1978(2009).
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; CP001185; ACJ75043.1; -; Genomic_DNA.
DR   RefSeq; WP_012579645.1; NC_011653.1.
DR   AlphaFoldDB; B7IG29; -.
DR   SMR; B7IG29; -.
DR   STRING; 484019.THA_555; -.
DR   PRIDE; B7IG29; -.
DR   EnsemblBacteria; ACJ75043; ACJ75043; THA_555.
DR   KEGG; taf:THA_555; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_0; -.
DR   OMA; CGEIMTM; -.
DR   OrthoDB; 177859at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000002453; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism;
KW   Reference proteome.
FT   CHAIN           1..551
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_1000146705"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   551 AA;  59873 MW;  861332D608F65B9E CRC64;
     MKTDIEIARE AKLEKITKIA EKIDISEEYV EPYGKYIAKV DLKIWEKVKN NKDGKLILVT
     AMTPTPAGEG KTTTSIGLSM ALNRLGKKSI VTLREPSLGP VFGIKGGAAG GGYSQVLPME
     NINLHFTGDI HAVSAAHNLI SAVIDAHIKF GNELGIDPTR IYWKRTIDMN DRALRNIVVG
     LGGSANGQPR EDGFIITAAS EIMAILCLAK DLKDLKERLS NIVVAQSYDK KLIKVKDLKI
     EGALAVLLKD AIKPNLVQTI ENTPAFVHGG PFANIAHGTN SIIATKLALK LSDYVVTEAG
     FAADLGAEKF LDFVSPTAGY DVNAVVVVAT IKALKYHGGV KKDELDNENV EAMLKGMENL
     RVHVENLKKY NVPVIVALNV FGSDTQRELD EFSKNCEIPH ALVYAFEKGG EGAVDLANLV
     LENIKESQYK PLITSEMSLE EKIETLAKEI YRAGNVIYTD KAKSKLKFLR KHGYDTLPVI
     VAKTQSSISD DPKKINAPSG YTFTIRDFEL SAGAGFIVAL AGDIMRMPGL SKIPNAVNID
     IDEEGNIIGL S