ID   FTHS_THEP1              Reviewed;         542 AA.
AC   A5ILJ8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Tpet_1054;
OS   Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS   RKU-1).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=390874;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermotoga petrophila RKU-1.";
RL   Submitted (MAY-2007) 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; CP000702; ABQ47071.1; -; Genomic_DNA.
DR   RefSeq; WP_011943601.1; NC_009486.1.
DR   AlphaFoldDB; A5ILJ8; -.
DR   SMR; A5ILJ8; -.
DR   STRING; 390874.Tpet_1054; -.
DR   EnsemblBacteria; ABQ47071; ABQ47071; Tpet_1054.
DR   KEGG; tpt:Tpet_1054; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_0; -.
DR   OMA; CGEIMTM; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000006558; 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..542
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_1000068799"
FT   BINDING         53..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   542 AA;  58628 MW;  E7AF395C77AFF3C8 CRC64;
     MKPIKEIADQ LGLKDDVLYP YGHYIAKIDH RFLKSLENRE DGKLILVTAV TPTPAGEGKT
     TTSIGLSMSL NRIGKKSIVT LREPSLGPTL GLKGGATGGG RSRVLPSDEI NLHFTGDMHA
     VASAHNLLAA VLDSHIKHGN ELKIDITRVF WKRTMDMNDR ALRSIVIGLG GSANGFPRED
     SFIITAASEV MAVLALSENM KDLKERLGKI IVALNTDRKI VRVSDLGIQG AMAVLLKDAI
     NPNLVQTTEG TPALIHCGPF ANIAHGTNSI IATKMAMKLS EYTVTEAGFG ADLGAEKFID
     FVSRVGGFYP NAAVLVATVR ALKYHGGADL KNIHEENLEA LKEGFKNLRV HLENLRKFNL
     PVVVALNRFI TDTEKEIAYV VKECEKLGVR VAVSEVFEKG SEGGVELAKA VTEAVKDVKP
     VYLYEMNDPV EKKIEILAKE IYRAGRVEFS DTAKNALKFI KKHGFDELPV IVAKTPKSIS
     HDPSLRGAPE GYTFVVSDLF VSAGAGFVVA LSGDINLMPG LPERPNALNM DVDDSGNIVG
     VS