ID   FTHS_LISW6              Reviewed;         560 AA.
AC   A0AJY2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=lwe1896;
OS   Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /
OS   NCTC 11857 / SLCC 5334 / V8).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=386043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8;
RX   PubMed=16936040; DOI=10.1128/jb.00758-06;
RA   Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA   Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA   Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA   Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT   "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT   genome reduction with Listeria innocua as compared to Listeria
RT   monocytogenes.";
RL   J. Bacteriol. 188:7405-7415(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; AM263198; CAK21314.1; -; Genomic_DNA.
DR   RefSeq; WP_011702663.1; NC_008555.1.
DR   AlphaFoldDB; A0AJY2; -.
DR   SMR; A0AJY2; -.
DR   STRING; 386043.lwe1896; -.
DR   PRIDE; A0AJY2; -.
DR   EnsemblBacteria; CAK21314; CAK21314; lwe1896.
DR   GeneID; 61189797; -.
DR   KEGG; lwe:lwe1896; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; CGEIMTM; -.
DR   OrthoDB; 177859at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000779; 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.
FT   CHAIN           1..560
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_0000300528"
FT   BINDING         69..76
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   560 AA;  60071 MW;  D37929796A267049 CRC64;
     MSNKVKSDIE IASKAEILPV TTIAKHLGLD ADALELYGKY KAKLSYDTIH SLKDQEPGKL
     VLVTAINPTP AGEGKSTVTV GLGDALSKKD KKTVIALREP SLGPTMGIKG GATGGGYAQV
     IPMEDINLHF TGDFHAITAA NNALSAFIDN HMQQGNELGI DGRRIVWKRV VDLNDRALRK
     VVVGLGGPVQ GVPREDGFDI TVASEIMAII CLASDLKDLK KRLSEIVIGY NYKKEPITVG
     EMGYEGALTL LLKDALKPNL VQTLEHTPAI VHGGPFANIA HGCNSVSATS TALRLGDYVV
     TEAGFGADLG AEKFLDIKVP ALGKAPDCVV IVATIRALKM HGGALKTELS EENVEALAKG
     FTNLQKHTES IQTFGIPYVV AINKFITDSD AEVAKLEALC EEHGIPFSLT EVWEKGGDGG
     LELADKVIAA VESGEADYNR IYDDAWSMEE KLEAIVTKVY GGIGVELSSK AQKQIVEFKK
     YGWDRYPICM AKTQYSLSDD PTLLGRPTDF VIHIREFIPK LGAGFVVALT GDVMTMPGLP
     KKPAALNMDV DENGNAQGLF