ID   FTHS_STRZJ              Reviewed;         556 AA.
AC   C1CEI6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=SPJ_1143;
OS   Streptococcus pneumoniae (strain JJA).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=488222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JJA;
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
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; CP000919; ACO19636.1; -; Genomic_DNA.
DR   RefSeq; WP_000845273.1; NC_012466.1.
DR   AlphaFoldDB; C1CEI6; -.
DR   SMR; C1CEI6; -.
DR   EnsemblBacteria; ACO19636; ACO19636; SPJ_1143.
DR   KEGG; sjj:SPJ_1143; -.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; CGEIMTM; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000002206; 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_1000185268"
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;  59642 MW;  BCF92FCF035409AF CRC64;
     MKTDIEIAQS IELKPIVDVV EKLGISYDDL ELYGKYKAKL SFDKIRAVES NPVGKLILVT
     AINPTPAGEG KSTLTIGLAD ALNKIGKKTM IAIREPSLGP VMGIKGGAAG GGYAQVLPME
     DINLHFTGDM HAITTANNAL SALIDNHLHQ GNELEIDQRR ILWKRVVDLN DRALRHVTVG
     LGGPLNGIPR EDGFDITVAS EIMAILCLAT DIEDLKRRLA NIVIGYRYDR TPVSVGDLQV
     EGALALILKD AIKPNLVQTI YGTPAFVHGG PFANIAHGCN SVLATTTALH LADYTVTEAG
     FGADLGAEKF LDIKTPNLPT SPDAVVIVAT LRALKMNGGV AKDALTEENV EAVRAGFANL
     KRHVENIRKF GIPAVVAINE FVSDTEAEIA VLKELCASID VPVELASVWA DGAEGGVALA
     ETVVKTIAEN PANYKRLYDN ALSVQEKIEK IVTEIYRGSK VNFEKKAQTQ IAQIVQNGWD
     KLPICMAKTQ YSFSDNPNAL GAPENFEITI RELVPKLGAG FIVALTGDVM TMPGLPKRPA
     ALNMDVESDG TVLGLF