ID   FTHS_DESRM              Reviewed;         567 AA.
AC   A4J0S6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Dred_0129;
OS   Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS   (Desulfotomaculum reducens).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=349161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-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; CP000612; ABO48679.1; -; Genomic_DNA.
DR   RefSeq; WP_011876523.1; NC_009253.1.
DR   AlphaFoldDB; A4J0S6; -.
DR   SMR; A4J0S6; -.
DR   STRING; 349161.Dred_0129; -.
DR   EnsemblBacteria; ABO48679; ABO48679; Dred_0129.
DR   KEGG; drm:Dred_0129; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; CGEIMTM; -.
DR   OrthoDB; 177859at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000001556; 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..567
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_0000333314"
FT   BINDING         68..75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   567 AA;  60771 MW;  246CA1784F2A0B40 CRC64;
     MKKVPSDLEI AQAHEMIPIA EIAKNIGLGE DDIDLYGKYK AKISLDVLRK FNDRAMGKLI
     DITAITPTPL GEGKTVTTIG LCQGLGKIGK KVITTLRQPS MGPVFGIKGG AAGGGYSQVV
     PMEDINIHFT GDIHAVEAAN NLLAAMIDTS ILLGNPLNID PMTVMWNRVL DTNDRALRDI
     VVGLGGKENG YPRQTSFDMA VASEVMAILA LAENLHDLRQ RLGRIIVAYT YDGKPVTAED
     LKAAGAMTVI MKEALKPNLV QTLEGQACIM HAGPFANIAH GNNSVLADKI ALNLADYVVT
     ESGFGSDLGM EKFMDIKCRQ SGLRPSCVVI TCTIRALKMH GGLGNVVAGK PLPEELTREN
     LPALEKGCAN LAHHIKVASY YGVPVVVSIN RFTPDTDAEV DLVRKKALEA GALGAYPITV
     WAEGGEGAIE LAEAVVAACE KTADFQLLYP DNLSIKEKIE VLATKVYNAD GVVFEPLAER
     KIKQFEDLGL GHLPICMAKT HLSISHDPAM KGLPKNYIFP IRDIRASVGA GFLYPLAGAM
     RTMPGLGSKP AAHNVDIDEY GRTVGLF