ID   FTHS_SYNWW              Reviewed;         555 AA.
AC   Q0AX38;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   18-JUN-2025, entry version 91.
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=Swol_1409;
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
OC   Syntrophomonadaceae; Syntrophomonas.
OX   NCBI_TaxID=335541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen;
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
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; CP000448; ABI68716.1; -; Genomic_DNA.
DR   RefSeq; WP_011640815.1; NC_008346.1.
DR   AlphaFoldDB; Q0AX38; -.
DR   SMR; Q0AX38; -.
DR   STRING; 335541.Swol_1409; -.
DR   KEGG; swo:Swol_1409; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OrthoDB; 9761733at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000001968; 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   FunFam; 3.30.1510.10:FF:000001; Formate--tetrahydrofolate ligase; 1.
DR   FunFam; 3.10.410.10:FF:000001; Putative formate--tetrahydrofolate ligase; 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; NF010030; PRK13505.1; 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..555
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_0000300551"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   555 AA;  59492 MW;  FCDEFF5E102A9BFA CRC64;
     MKTDVEIAQS AKMQPITEIA DRIGIEPNEL ELYGSYKAKI SLDIMKRIED KPQGKLVLVT
     AISPTPAGEG KTTTTIGLGQ ALNKIGKKAI VALREPSLGP VFGIKGGATG GGYAQVVPME
     DINLHFTGDI HAVTTAHNLL AALMDNHLHQ GNELDIDSRQ IVWRRVMDLN ERVLRNIVLG
     LGGRINGVPR ESGFDISVAS EVMAALCLAT DLMDLKERFA KIVVAYSQQG QAITAGDLKA
     AGSMALLMKD AIKPNLVQTL ENTPAFIHGG PFANIAHGAN SIVATRLGVK LADYMVTEAG
     FGADLGAEKF FNIVCRYGKL VPDAVVLVAS IRALKHHGGV KKDKLGEENL EALAQGMENL
     KKHLENIQKF GVPAVVALNE FPSDTSKEID YVFSQCAAMQ TAVSISRVWA QGGEGGIDLA
     EKLVLATEQG SQFKFLYELN QPLKNKIETI CREIYGAGSV KYAAEAKRML QKYEESGFGD
     LPVCIAKTQY SLSDNAQLLG RPTGFEVNIR QVKLSAGAGF VVALAGDIMT MPGLGKVPAA
     ENIDIKPDGE IVGLF
//