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FTHS_NEIM0
ID   FTHS_NEIM0              Reviewed;         558 AA.
AC   A9M1J1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=NMCC_0383;
OS   Neisseria meningitidis serogroup C (strain 053442).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=374833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=053442;
RX   PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004;
RA   Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z.,
RA   Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z.,
RA   Liang X., Xu J., Jin Q.;
RT   "Characterization of ST-4821 complex, a unique Neisseria meningitidis
RT   clone.";
RL   Genomics 91:78-87(2008).
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; CP000381; ABX72589.1; -; Genomic_DNA.
DR   RefSeq; WP_012221285.1; NC_010120.1.
DR   AlphaFoldDB; A9M1J1; -.
DR   SMR; A9M1J1; -.
DR   EnsemblBacteria; ABX72589; ABX72589; NMCC_0383.
DR   KEGG; nmn:NMCC_0383; -.
DR   HOGENOM; CLU_003601_3_3_4; -.
DR   OMA; CGEIMTM; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000001177; 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..558
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_1000087652"
FT   BINDING         66..73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   558 AA;  59103 MW;  296C2FC7EC4FEFD3 CRC64;
     MSFKTDAEIA QSSTMRPIGE IAAKLGLNAD NIEPYGHYKA KINPAEAFKL PQKQGRLILV
     TAINPTPAGE GKTTVTIGLA DALRHIGKDS VIALREPSLG PVFGVKGGAA GGGYAQVLPM
     EDINLHFTGD FHAIGAANNL LAAMLDNHIY QGNELDIDPK RVLWRRVVDM NDRQLRNIID
     GMGKPVDGVM RPDGFDITVA SEVMAVFCLA KDISDLKERL GNILVAYAKD GSPVYAKDLK
     ANGAMAALLK DAIKPNLVQT IEGTPAFVHG GPFANIAHGC NSVTATRLAK HLADYAVTEA
     GFGADLGAEK FCDIKCRLAG LKPDAAVVVA TVRALKYNGG VERANLGEEN LDALEKGLPN
     LLKHISNLKN VFGLPVVVAL NRFVSDSDAE LAMIEKACAE HGVEVSLTEV WGKGGAGGAD
     LARKVVNAIE SQTNNFGFAY DVELGIKDKI RAIAQKVYGA EDVDFSAEAS AEIASLEKLG
     LDKMPICMAK TQYSLSDNAK LLGCPEGFRI AVRGITVSAG AGFIVALCGN MMKMPGLPKV
     PAAEKIDVDE HGVIHGLF
 
 
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