ID   FTHS_LIMRJ              Reviewed;         553 AA.
AC   B2G5A9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=LAR_0125;
OS   Limosilactobacillus reuteri (strain JCM 1112) (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=557433;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 1112;
RX   PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA   Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA   Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA   Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA   Hattori M.;
RT   "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT   fermentum reveal a genomic island for reuterin and cobalamin production.";
RL   DNA Res. 15:151-161(2008).
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; AP007281; BAG24641.1; -; Genomic_DNA.
DR   RefSeq; WP_003669710.1; NC_010609.1.
DR   AlphaFoldDB; B2G5A9; -.
DR   SMR; B2G5A9; -.
DR   GeneID; 66470212; -.
DR   KEGG; lrf:LAR_0125; -.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; CGEIMTM; -.
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; 3.40.50.300; -; 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.
FT   CHAIN           1..553
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_1000196812"
FT   BINDING         62..69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   553 AA;  60252 MW;  191BBFE9E0FB534D CRC64;
     MTDIEIADQA TLEPITEIAE KLGLSEDEIE QYGKYKAKID LNVKPLPDKK HKLILVTSIN
     PTPAGEGKST VLIGLGDALN QLNYQTTIAM REPSMGPVFG IKGGATGGGY SQVVPMEDIN
     LNFTGDLHAL TSANNTLAAL IDNYIMRDNA MNLDPRRIIW KRVEDVNDRA LRNVVTGLGG
     PMAGVPRETG FDITAASELM AILCLSTSLH DLKERISRIV VGYTYDKEPV TVGQLNFQDA
     ITIILKDALK PNLVQTLDHT PTIVHGGPFA NIAHGCNSVL ATQTALNLSD YTVTEAGFGA
     DLGGEKFLDI KQRVLGKHPD AIVIVATVRA LEYNGGAKLA DLNEENLDAL KKGMANLNRH
     IKNMQLYGLP IVVAINHFVS DTDKEIQMIK DDCAKQNVEA ILTDAWAKGG KGTHDLANKV
     VELADSPSEF THIYDVQVDD LQTKLEKIAK QIYGAKEVSF SRKAQNQLKR FAKYGWNDLP
     VCIAKTQYSF TDDQKQLGAP TDFTFHIREL VPKIGAGFVV ALAGNMMTMP GLPKEPAAVN
     MMIDDNGKIT GLF