ID   DHPS_STRP3              Reviewed;         266 AA.
AC   P0DB08; Q8K7K8;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Dihydropteroate synthase;
DE            Short=DHPS;
DE            EC=2.5.1.15;
DE   AltName: Full=Dihydropteroate pyrophosphorylase;
GN   Name=folP; OrderedLocusNames=SpyM3_0760;
OS   Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=198466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-595 / MGAS315;
RX   PubMed=12122206; DOI=10.1073/pnas.152298499;
RA   Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA   Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA   Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT   "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT   encoded toxins, the high-virulence phenotype, and clone emergence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002).
CC   -!- FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with
CC       6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-
CC       dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
CC       {ECO:0000250|UniProtKB:P0AC13}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate =
CC         7,8-dihydropteroate + diphosphate; Xref=Rhea:RHEA:19949,
CC         ChEBI:CHEBI:17836, ChEBI:CHEBI:17839, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:72950; EC=2.5.1.15;
CC         Evidence={ECO:0000250|UniProtKB:P0AC13};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P0AC13};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-
CC       dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
CC       dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
CC   -!- SUBUNIT: Homodimer or homotrimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DHPS family. {ECO:0000305}.
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DR   EMBL; AE014074; AAM79367.1; -; Genomic_DNA.
DR   RefSeq; WP_011054468.1; NC_004070.1.
DR   AlphaFoldDB; P0DB08; -.
DR   SMR; P0DB08; -.
DR   EnsemblBacteria; AAM79367; AAM79367; SpyM3_0760.
DR   KEGG; spg:SpyM3_0760; -.
DR   HOGENOM; CLU_008023_0_2_9; -.
DR   OMA; FSIDTYH; -.
DR   UniPathway; UPA00077; UER00156.
DR   Proteomes; UP000000564; Chromosome.
DR   GO; GO:0004156; F:dihydropteroate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00739; DHPS; 1.
DR   Gene3D; 3.20.20.20; -; 1.
DR   InterPro; IPR045031; DHP_synth.
DR   InterPro; IPR006390; DHP_synth_dom.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
DR   InterPro; IPR000489; Pterin-binding_dom.
DR   PANTHER; PTHR20941; PTHR20941; 1.
DR   Pfam; PF00809; Pterin_bind; 1.
DR   SUPFAM; SSF51717; SSF51717; 1.
DR   TIGRFAMs; TIGR01496; DHPS; 1.
DR   PROSITE; PS00792; DHPS_1; 1.
DR   PROSITE; PS00793; DHPS_2; 1.
DR   PROSITE; PS50972; PTERIN_BINDING; 1.
PE   3: Inferred from homology;
KW   Folate biosynthesis; Magnesium; Metal-binding; Transferase.
FT   CHAIN           1..266
FT                   /note="Dihydropteroate synthase"
FT                   /id="PRO_0000168234"
FT   DOMAIN          12..260
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT   BINDING         19
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WND1"
FT   BINDING         59
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         93
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         112
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         176
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         212
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         248..250
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
SQ   SEQUENCE   266 AA;  28755 MW;  B3F79D5BC5445ACD CRC64;
     MKIGKFVIEG NAAIMGILNV TPDSFSDGGS YTTVQKALDH VEQMIADGAK IIDVGGESTR
     PGCQFVSATD EIDRVVPVIK AIKENYDILI SIDTYKTETA RAALEAGADI LNDVWAGLYD
     GQMFALAAEY DAPIILMHNQ DEEVYQEVTQ DVCDFLGNRA QAALDAGVPK NNIWIDPGFG
     FAKSVQQNTE LLKRLDRVCQ LGYPVLFGIS RKRVVDALLG GNTKAKERDG ATAALSAYAL
     GKGCQIVRVH DVKANQDIVA VLSQLM