ID   FTHS_AGARV              Reviewed;         556 AA.
AC   C4ZBG8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, 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=EUBREC_1958;
OS   Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835
OS   / VPI 0990) (Eubacterium rectale).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lachnospiraceae incertae sedis.
OX   NCBI_TaxID=515619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / LMG 30912 / VPI
RC   0990;
RX   PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA   Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA   Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA   Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA   Hettich R.L., Gordon J.I.;
RT   "Characterizing a model human gut microbiota composed of members of its two
RT   dominant bacterial phyla.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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; CP001107; ACR75700.1; -; Genomic_DNA.
DR   RefSeq; WP_012742797.1; NC_012781.1.
DR   AlphaFoldDB; C4ZBG8; -.
DR   SMR; C4ZBG8; -.
DR   STRING; 515619.EUBREC_1958; -.
DR   EnsemblBacteria; ACR75700; ACR75700; EUBREC_1958.
DR   KEGG; ere:EUBREC_1958; -.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; TRQGFSK; -.
DR   OrthoDB; 177859at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000001477; 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.
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..556
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_1000215436"
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;  59751 MW;  068E29AC30E75992 CRC64;
     MKTDIQIAQE ATMLPIKDVA ASIGIEEDDL ELYGKYKAKI SDELINRTKK NPDGKLILVT
     AINPTPAGEG KTTTSVGLGE AFGRLGKKAL IALREPSLGP CFGIKGGAAG GGYAQVVPME
     DLNLHFTGDF HAITSANNLL AALLDNHIQQ GNELGIDPRQ IVWKRCMDMN DRVLRNIVVG
     LGSKMDGMVR EDHFVITVAS EIMAILCLAD DMADLKKRLG RIIVAYTFDG KPVTADDLQA
     TGSMAALLKD ALKPNLIQTL EHTPAIVHGG PFANIAHGCN SVRATKTALK LADYVITEAG
     FGADLGAEKF FDIKCRMAGL KPDAVVLVAT IRALKYNGGV PKDELSSENL DALKAGIVNL
     EKHIENLHKF GVPVVVTLNS FVTDTKAETD FVEQFCKERG CEFALSEVWE KGGEGGIDLA
     NKVLETIEHK ESNFKVLYDD SLSLKEKIET VAKEIYGADG VTYSPAAERE LKRITDLGMG
     DFPVCMAKTQ YSLSDDAKKL GRPSGFKINV REVYASAGAG FVVAVNGSIM TMPGLSKKPA
     AYGIDVDDNG VITGLF