ID   FTHS_CAMC1              Reviewed;         549 AA.
AC   A8Z6G1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=Ccon26_04790;
GN   ORFNames=CCC13826_1498;
OS   Campylobacter concisus (strain 13826).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13826;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., On S., Nelson K.E.;
RT   "Genome sequence of Campylobacter concisus 13826 isolated from human
RT   feces.";
RL   Submitted (OCT-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; CP000792; ABW74745.1; -; Genomic_DNA.
DR   RefSeq; WP_048809763.1; NC_009802.2.
DR   AlphaFoldDB; A8Z6G1; -.
DR   SMR; A8Z6G1; -.
DR   STRING; 360104.CCC13826_1498; -.
DR   EnsemblBacteria; ABW74745; ABW74745; CCC13826_1498.
DR   KEGG; cco:CCC13826_1498; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_7; -.
DR   OMA; CGEIMTM; -.
DR   OrthoDB; 177859at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000001121; 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.
FT   CHAIN           1..549
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_1000073554"
FT   BINDING         60..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   549 AA;  59528 MW;  2BC4D90EA935325E CRC64;
     MLSDIEITHQ TKLEHISKVA AKLGLNEDEL ELYGKFKAKI SPRLEPSNSK LILVTATNPT
     PYGEGKTTMS IGLADALNSL NKKVCLALRE PSLGPVFGIK GGAAGGGYSQ LAPMEDLNLH
     FTGDFHAITS ANNLISAMID NSLYQENPLK IEKILWKRCM DMNDRALRFI TVGQGGRTDG
     VPREDGFNIT AASEIMAVLC LATSLSDLKE RVANIMVAYD SDKKPIYVRD LGCEDAVCIL
     LKDAIKPNLF QTLEHTPTLV HGGPFANIAH GCNSVIATKT ALNLADYVIT EAGFGSELGA
     EKFLDIKCRV AEIKPSAVVL VSTIRSLKYN GEANKDEITK PDMNALKKGI ENLGGHIENL
     KGKFGQNVVV ALNKFGFDTD EEINFVKEYC QKLGIEVAVC ENFLKGGKGA LELAELVLKA
     CDKPSKINFT YEMSDDTKTK IEKVAKEIYG AGEVVFEEAA LKKLEMIKEL NLSHLPVCIA
     KTQYSFSDDA KLLGRAKGFT FSVKDLDIRT GAGFIVAVCG KIMLMPGLPK VPAAVNMKID
     AEGKIDGLS