FTHS_METPP
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 03-AUG-2022, entry version 77.
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=Mpe_A3264;
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; 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 = (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; 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 PRIDE; A2SKX8; -.
DR EnsemblBacteria; ABM96217; ABM96217; Mpe_A3264.
DR KEGG; mpt:Mpe_A3264; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_4; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
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; 3.40.50.300; -; 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..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
