ID   FTHS_STRMU              Reviewed;         556 AA.
AC   Q59925; Q59926;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 126.
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}; Synonyms=fthS;
GN   OrderedLocusNames=SMU_1073;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=JH1005;
RX   PubMed=9045814; DOI=10.1128/jb.179.5.1563-1572.1997;
RA   Crowley P.J., Gutierrez J.A., Hillman J.D., Bleiweis A.S.;
RT   "Genetic and physiologic analysis of a formyl-tetrahydrofolate synthetase
RT   mutant of Streptococcus mutans.";
RL   J. Bacteriol. 179:1563-1572(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 139-296.
RC   STRAIN=NG8;
RX   PubMed=8763945; DOI=10.1128/jb.178.14.4166-4175.1996;
RA   Gutierrez J.A., Crowley P.J., Brown D.P., Hillman J.D., Youngman P.,
RA   Bleiweis A.S.;
RT   "Insertional mutagenesis and recovery of interrupted genes of Streptococcus
RT   mutans by using transposon Tn917: preliminary characterization of mutants
RT   displaying acid sensitivity and nutritional requirements.";
RL   J. Bacteriol. 178:4166-4175(1996).
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; U39612; AAB49329.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN58771.1; -; Genomic_DNA.
DR   EMBL; U48882; AAC44499.1; -; Genomic_DNA.
DR   RefSeq; NP_721465.1; NC_004350.2.
DR   RefSeq; WP_002262267.1; NC_004350.2.
DR   AlphaFoldDB; Q59925; -.
DR   SMR; Q59925; -.
DR   STRING; 210007.SMU_1073; -.
DR   PRIDE; Q59925; -.
DR   EnsemblBacteria; AAN58771; AAN58771; SMU_1073.
DR   KEGG; smu:SMU_1073; -.
DR   PATRIC; fig|210007.7.peg.960; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; CGEIMTM; -.
DR   PhylomeDB; Q59925; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000002512; 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;
KW   Reference proteome.
FT   CHAIN           1..556
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_0000199386"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
FT   CONFLICT        25
FT                   /note="F -> I (in Ref. 1; AAB49329)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   556 AA;  59734 MW;  E86BE44B307C099D CRC64;
     MKTDIEIAQS VDLRPITNVV KKLGFDFDDL ELYGKYKAKL TFDKIKAVEE NAPGKLVLVT
     AINPTPAGEG KSTITIGLAD ALNKIGKKTM IAIREPSLGP VMGIKGGAAG GGYAQVLPME
     DINLHFTGDM HAITTANNAL SALIDNHLHQ GNELGIDQRR IIWKRVVDLN DRALRHVTVG
     LGSPINGIPR EDGFDITVAS EIMAILCLAT NVEDLKERLA NIVIGYRFDR SPVYVRDLEV
     QGALALILKE AIKPNLVQTI YGTPAFVHGG PFANIAHGCN SVLATSTALR LADYTITEAG
     FGADLGAEKF LDIKAPNLPT SPDAVVIVAT IRALKMNGGV AKDALNQENV EAVKAGFANL
     ARHVENMRKY GVPVVVAINE FITDTNDEIA VLRNLCAAID VPVELASVWA NGADGGVDLA
     NTLINTIENN PSHYKRLYDN NLSVEEKVTE IAKEIYRADK VIFEKKAKTQ IAQIVKNGWD
     NLPICMAKTQ YSFSDDPKLL GAPTGFDITI RELVPKLGAG FIVALTGDVM TMPGLPKKPA
     ALNMDVAADG TALGLF