ID   FTHS_LACJO              Reviewed;         557 AA.
AC   Q74JC1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=LJ_1188;
OS   Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=257314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNCM I-1225 / La1 / NCC 533;
RX   PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA   Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA   Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA   Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT   "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT   johnsonii NCC 533.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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; AE017198; AAS09009.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q74JC1; -.
DR   SMR; Q74JC1; -.
DR   STRING; 257314.LJ_1188; -.
DR   EnsemblBacteria; AAS09009; AAS09009; LJ_1188.
DR   KEGG; ljo:LJ_1188; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; VDNYIYQ; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000581; 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   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;
KW   Reference proteome.
FT   CHAIN           1..557
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_0000199353"
FT   BINDING         66..73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   557 AA;  60475 MW;  7E615C183F9F3393 CRC64;
     MKSDIEIAQD TKELPITEIA KKVDLQPDEI ELYGNDKAKI SWKGINRIKQ GKKLGKLILV
     TSISPTPAGE GKSTITIGLG DAISNQLHKN TLIALREPSM GPVFGLKGGA TGGGYAQIIT
     MEDINLHFTG DMHALTSAID TLAALVDNYI YQDNSLELDP NRILLKRGID VNDRTLRKIT
     IGQGSRFNGI EHEASFAITV ANELMAILCL ATDIDDLKKR IGNMLVGFSV KDEPVYVKDL
     GFEGAIAALL STALKPNLVQ TLEHTPAIVH GGPFANIAHG ANSVIATNTA LHLSDYVLTE
     AGFGADLGGQ KFMDFVSNHL DKRPDAVVVV ATVRALKYQA EETTDHLDEE NIPALEKGFE
     NLKRHMENMA HYGVPVIVLI NKFASDTEQE LSKLKELVKA DGFECEVVSY HDEGSKGGIK
     AAEKVVELTN KASDFTSVYE PTDSVEEKIS KIAHNIYHAK DIEYSDKAKD QLAEIKKMGK
     DNLPVIMAKT QYSFTDKKSI LGAPKDFTLH VKNLALKNGA GFIVVATGSI LDMPGLPKYP
     AALDIDVDNN GKISGLF