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FTHS_STRA3
ID   FTHS_STRA3              Reviewed;         556 AA.
AC   Q8E5E3;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=gbs1089;
OS   Streptococcus agalactiae serotype III (strain NEM316).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=211110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEM316;
RX   PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA   Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA   Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT   "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT   neonatal disease.";
RL   Mol. Microbiol. 45:1499-1513(2002).
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; AL766848; CAD46748.1; -; Genomic_DNA.
DR   RefSeq; WP_000845316.1; NC_004368.1.
DR   AlphaFoldDB; Q8E5E3; -.
DR   SMR; Q8E5E3; -.
DR   STRING; 211110.gbs1089; -.
DR   EnsemblBacteria; CAD46748; CAD46748; CAD46748.
DR   KEGG; san:gbs1089; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; CGEIMTM; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000823; 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_0000199384"
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;  59933 MW;  562ECB49DF82D336 CRC64;
     MKTDIEIAQS VALKPIAEIV EQVGIGFDDI ELYGKYKAKL SFDKIEAVRS QKVGKLILVT
     AINPTPAGEG KSTMSIGLAD ALNKIGKKTM IALREPSLGP VMGIKGGAAG GGYAQVLPME
     DINLHFTGDM HAITTANNAL SALLDNHIHQ GNELDIDQRR VIWKRVVDLN DRALRQVIVG
     LGSSVNGIPR EDGFDITVAS EIMAILCLAT DLSDLKKRLS NIVVAYSRDR KPIYVKDLKI
     EGALTLILKD AIKPNLVQTI YGTPALVHGG PFANIAHGCN SVLATSTALR LADYVVTEAG
     FGADLGAEKF LDIKTPNLPT SPDAIVIVAT LRALKMHGGV SKEDLSQENV KAVKRGFTNL
     ERHVNNMRQY GVPVVVAINQ FTADTESEIA TLKTLCSNID VAVELASVWE DGADGGLELA
     QTVANVIETQ SSNYKRLYND EDTIEEKIKK IVTKIYGGNK VHFGPKAQIQ LKEFSDNGWD
     KMPICMAKTQ YSFSDNPNLL GAPTDFDITV REFVPKTGAG FIVALTGDVL TMPGLPKKPA
     ALNMDVLEDG TAIGLF
 
 
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