FTHS_STRE4
ID FTHS_STRE4 Reviewed; 556 AA.
AC C0M9N3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=SEQ_1075;
OS Streptococcus equi subsp. equi (strain 4047).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553482;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4047;
RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA Maskell D.J., Parkhill J., Waller A.S.;
RT "Genomic evidence for the evolution of Streptococcus equi: host
RT restriction, increased virulence, and genetic exchange with human
RT pathogens.";
RL PLoS Pathog. 5:E1000346-E1000346(2009).
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; FM204883; CAW93710.1; -; Genomic_DNA.
DR RefSeq; WP_012679495.1; NC_012471.1.
DR AlphaFoldDB; C0M9N3; -.
DR SMR; C0M9N3; -.
DR EnsemblBacteria; CAW93710; CAW93710; SEQ_1075.
DR KEGG; seu:SEQ_1075; -.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001365; 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..556
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_1000185264"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 556 AA; 59518 MW; 436B91F0DFFEEE9A CRC64;
MKSDIEIAQS VPLKPITEIV KKVGIDADDL ELYGNYKAKL SFEKIKSVED NKPGKLILVT
AINPTPAGEG KSTMSIGLAD ALTKIGKKTM LALREPSLGP VMGIKGGAAG GGYAQVLPME
DINLHFTGDM HAITTAHNAL SALIDNHLQQ GNELGIDPRR IIWKRVLDLN DRSLRQVIVG
LGSPVNGVPR EDGFDITVAS EVMAILCLAT DLKDLKARLA NIVIAYRYDK SPVYVRDLKV
EGALALILKD AIKPNLVQTI YGTPAFVHGG PFANIAHGCN SVLATSTALR LADYTVTEAG
FGADLGAEKF LNIKTPNLPK APDAVVIVAT LRALKMHGGV AKADLTFENT AAVRSGFANL
KRHVENIRKF NIPIVVAINE FVTDTKAEIQ VLKELCAEIA VPVELASVWA KGADGGIALA
NAVVKAITEE SAAYKRLYAD KDSLEEKLKA IVTEIYGGRA VQFGPKAKNQ LKQFAQFGWD
QLPVCMAKTQ YSFSDDPSLL GAPDQFDITI RELVPKTGAG FIVALTGDVM TMPGLPKIPA
AMKMDVTEDG TAVGLF