ID   FTHS_CLOAC              Reviewed;         556 AA.
AC   P13419;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   27-MAR-2024, entry version 89.
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};
OS   Clostridium acidurici (Gottschalkia acidurici).
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Gottschalkiaceae;
OC   Gottschalkia.
OX   NCBI_TaxID=1556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2838464; DOI=10.1128/jb.170.7.3255-3261.1988;
RA   Whitehead T.R., Rabinowitz J.C.;
RT   "Nucleotide sequence of the Clostridium acidiurici ('Clostridium acidi-
RT   urici') gene for 10-formyltetrahydrofolate synthetase shows extensive amino
RT   acid homology with the trifunctional enzyme C1-tetrahydrofolate synthase
RT   from Saccharomyces cerevisiae.";
RL   J. Bacteriol. 170:3255-3261(1988).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (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; M21507; AAA53187.1; -; Genomic_DNA.
DR   PIR; A28185; A28185.
DR   AlphaFoldDB; P13419; -.
DR   SMR; P13419; -.
DR   OMA; KFWNLKC; -.
DR   BRENDA; 6.3.4.3; 1454.
DR   UniPathway; UPA00193; -.
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; 3.30.1510.10; 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   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.
FT   CHAIN           1..556
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_0000199338"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   556 AA;  59589 MW;  72D9D485863F0334 CRC64;
     MKTDIQIAQE AQMKHIKDVA ELIDIHEDDL ELYGKYKAKV SLDVLDQLKD KPDGKLVLVT
     AINPTPAGEG KTTTNIGLSM GLNKLGKKTS TALREPSLGP SFGVKGGAAG GGYAQVVPMA
     DINLHFTGDF HAITSAHSLL AALVDNHLHH GNALRIDTNR IVWKRVVDMN DRALRKIVVG
     LGGKAQGITR EDGFDITVAS EIMAILCLAN DREDLKERLG NMVVAYNVDG DAVRAKDLEA
     QGALTLILKD AINPNIVQTL ENTPAFIHGG PFANIAHGCN SVLATKLALK TGDYAVTEAG
     FGADLGAEKF FDIKCRYAGL NPDVAVIVAT VRALKMHGGV AKEDLGTENL DALAKGMTNL
     ERHIENVAKF GVPSVVAINA FPTDTEAEKQ LVFDKCKEMG VDVAISDVFA KGGDGGVELA
     QKVIDVCENK KSDFKVLYDV EESIPEKITK IAKEIYRADK VNFSKAAKKQ IAELEKLGLD
     KLPICMAKTQ YSFSDDPALL GAPEGFELTI RDLELAAGAG FIVALTGDIM RMPGLPKVPA
     ANRMDVLPNG EIIGLF
//