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