ID   FTHS_DESAH              Reviewed;         591 AA.
AC   C0QAX9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   18-JUN-2025, entry version 71.
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};
GN   OrderedLocusNames=HRM2_16700;
OS   Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS   HRM2) (Desulfobacterium autotrophicum).
OC   Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
OC   Desulfobacterales; Desulfobacteraceae; Desulforapulum.
OX   NCBI_TaxID=177437;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43914 / DSM 3382 / VKM B-1955 / HRM2;
RX   PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA   Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA   Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA   Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA   Meyerdierks A., Gottschalk G., Amann R.;
RT   "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT   reducer oxidizing organic carbon completely to carbon dioxide.";
RL   Environ. Microbiol. 11:1038-1055(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + formate + ATP = (6R)-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:195366, ChEBI:CHEBI:456216;
CC         EC=6.3.4.3; 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; CP001087; ACN14778.1; -; Genomic_DNA.
DR   RefSeq; WP_015903565.1; NC_012108.1.
DR   AlphaFoldDB; C0QAX9; -.
DR   SMR; C0QAX9; -.
DR   STRING; 177437.HRM2_16700; -.
DR   KEGG; dat:HRM2_16700; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_7; -.
DR   OrthoDB; 9761733at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000442; 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-UniRule.
DR   CDD; cd00477; FTHFS; 1.
DR   Gene3D; 3.30.1510.10; Domain 2, N(10)-formyltetrahydrofolate synthetase; 1.
DR   Gene3D; 3.10.410.10; Formyltetrahydrofolate synthetase, domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; NF010032; PRK13507.1; 1.
DR   Pfam; PF01268; FTHFS; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..591
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_1000215434"
FT   BINDING         74..81
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   591 AA;  63927 MW;  136606B37A755835 CRC64;
     MALDPTKHAD WEIAQDAEKD MLTIYEIGEK LGLTKEELLP QGHYIAKIDF RAVLARLKDK
     PDGKYIDVTA ITPTPLGEGK STSSMGLVQG LGKLGKSVCA AIRQPSGGPT MNIKGSAAGG
     GLAQCIPLTP FSLGFTGDIN AIMNAHNLAM VALTSRMQHE RNYTDEQLER LSGMKRIDID
     PTRVEMGWIM DFCCQSLRNI IIGIDGVNGK SDGYMMKSKF GIAVSSEVMA ILAVAKDLKD
     MRERMGKIVV AYTKKGKPVT TEDLQVAGAM TAWMVDALNP SLIQTLEGQP VLVHAGPFAN
     IAIGQSSIIA DRVGLKLADY HVTESGFGAD IGFEKFWNLK CRFSGLKPDC AVIVATIRAL
     KCHGGAPVPV PGKPMPEEYN TESVEWVEKG CANLLHHIRN VRKAGISPVV CINAFYSDTD
     AEIAKVRELS EAEGARVALS RHWEKGGDGA IEFAETVIEA CEEETEFKFL YELDMPLKER
     IELIAKEVYG ADGVDYSNEA NASLARIQAD PELAKLGMCM VKTHLSLSDN PSLKGVPTGW
     RLMIREVLTY GGAGFIVPVA GTISLMPGTG SNPAFKRVDV DCETGKVEGV F
//