FTHS_LIGS1
ID FTHS_LIGS1 Reviewed; 552 AA.
AC Q1WTW0;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=LSL_0842;
OS Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=362948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCC118;
RX PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT "Multireplicon genome architecture of Lactobacillus salivarius.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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; CP000233; ABD99652.1; -; Genomic_DNA.
DR RefSeq; WP_011475989.1; NC_007929.1.
DR RefSeq; YP_535735.1; NC_007929.1.
DR AlphaFoldDB; Q1WTW0; -.
DR SMR; Q1WTW0; -.
DR STRING; 362948.LSL_0842; -.
DR EnsemblBacteria; ABD99652; ABD99652; LSL_0842.
DR KEGG; lsl:LSL_0842; -.
DR PATRIC; fig|362948.14.peg.916; -.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000006559; 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..552
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000293043"
FT BINDING 62..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 552 AA; 59469 MW; 60151621C7ABA759 CRC64;
MKDIEIAQKS EMLPITEVAQ KVGLTADEIE QYGKYKAKIS LPLSAREQTK RKLVLVTAIN
PTPAGEGKST VTVGLGDAFS LLNKKVMIAL REPSLGPVMG MKGGATGGGY SQVVPMEDIN
LHFTGDMHAL TTANNTLAAL IDNHIYQGNK LNIDQRRVIW KRVLDINDRA LRHVVIGLGG
ATQGIPREDG FDITVASELM AILCLSKDIS DLKKRIGQIV IGYNFDKEPV TVDQLGVTGA
ITLLLKDACK PNLVQTLAHT PAIVHGGPFA NIAHGCNSVL ATQTALNLAD YTITEAGFGA
DLGAEKFLDI KTPVLGKTPD TIVIVATARA LKMNGGVAKD NLDEENVAAV EQGFANLKKH
IQSMKRYNVP VVVAINKFTQ DTDAELAKIV ELCEQDDTKA IVADVWAKGG EGATELAKAV
IESCDNDQEF TRLYNSDDSV EEKINKIVTE IYGGDGVEFS AKAKRQLRQF EKLGWNHLPV
CMAKTQYSLS DNAKVLGAPK GFKIHVREFV PKLGAQFLVA LTGNILTMPG LPKVPAADGM
DVDENGKISG LY
