ID   FTHS_METPP              Reviewed;         561 AA.
AC   A2SKX8;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
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};
GN   OrderedLocusNames=Mpe_A3264;
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Methylibium.
OX   NCBI_TaxID=420662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX   PubMed=17158667; DOI=10.1128/jb.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-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:195366, ChEBI:CHEBI:456216;
CC         EC=6.3.4.3; 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; CP000555; ABM96217.1; -; Genomic_DNA.
DR   RefSeq; WP_011830840.1; NC_008825.1.
DR   AlphaFoldDB; A2SKX8; -.
DR   SMR; A2SKX8; -.
DR   STRING; 420662.Mpe_A3264; -.
DR   KEGG; mpt:Mpe_A3264; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_4; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000366; 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; 3.30.1510.10; Domain 2, N(10)-formyltetrahydrofolate synthetase; 1.
DR   Gene3D; 3.10.410.10; Formyltetrahydrofolate synthetase, domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; P-loop containing nucleoside triphosphate hydrolases; 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..561
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_0000293046"
FT   BINDING         66..73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   561 AA;  60140 MW;  8114C016F8B97EE1 CRC64;
     MASDIEIAQK ATLRRITQVA SDKLGIADEH LEPYGHYKAK LSLDYVDSLK DRPNGKLILV
     TAISPTPAGE GKTTTTVGLG DALNRIGKKT LVCLREPSLG PVFGMKGGAA GGGHAQVVPM
     EDINLHFTGD FNAIQLANNL LAAMIDNHIH HGNELDIDVR RITWKRVLDM NDRALRDITC
     SLGGPGNGYP REDGFDIVVA SEVMAIFCLA TSIQDLKERL GNIVVGYTRQ QKPVTARDLK
     AHGAMTVLLK DALKPNLVQT LENNPAILHG GPFANIAHGC NSVIATQTSL KLADYVVTEA
     GFGADLGAEK FIDIKCRKSG LRPDAVVLVA TIRALKFHGG VDVKELNTEN LDALEKGIAN
     IERHVANIRE HYGLPCVVSI NNFTFDTPAE LKLLQDRMAK HEVPVIVARH WAEGGKGAED
     VARAVVEIVE KGQSGAAGFK FVYDESLPLM DKITAIATKI YGAAKVNASA KVAGEIKKLQ
     DAGYGHYPVC VAKTQYSFST NPSARGAPSG HTIDIREVRL AAGAEFIVMI CGDVMTMPGL
     PKVPSAEKID LGDDGKVVGL F
//