ID   DHPS_STRPY              Reviewed;         266 AA.
AC   P0C0G0; O33724;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Dihydropteroate synthase;
DE            Short=DHPS;
DE            EC=2.5.1.15;
DE   AltName: Full=Dihydropteroate pyrophosphorylase;
GN   Name=folP;
OS   Streptococcus pyogenes.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G56;
RX   PubMed=9593127; DOI=10.1128/aac.42.5.1062;
RA   Swedberg G., Ringertz S., Skoeld O.;
RT   "Sulfonamide resistance in Streptococcus pyogenes is associated with
RT   differences in the amino acid sequence of its chromosomal dihydropteroate
RT   synthase.";
RL   Antimicrob. Agents Chemother. 42:1062-1067(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G56;
RX   PubMed=8304179; DOI=10.1007/978-1-4615-2960-6_113;
RA   Swedberg G., Fermer C., Skoeld O.;
RT   "Point mutations in the dihydropteroate synthase gene causing sulfonamide
RT   resistance.";
RL   Adv. Exp. Med. Biol. 338:555-558(1993).
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.
CC   -!- SIMILARITY: Belongs to the DHPS family. {ECO:0000305}.
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DR   EMBL; AJ000685; CAA04238.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C0G0; -.
DR   SMR; P0C0G0; -.
DR   SABIO-RK; P0C0G0; -.
DR   UniPathway; UPA00077; UER00156.
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_0000168232"
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;  28515 MW;  C6BC402F07CFDF36 CRC64;
     MKIGKFVIDG NAAIMGILNV TPDSFSDGGS YTTVQKVLQQ VDQLIAGGAK IIDVGGESTR
     PGYQFVSAAD EIERVVPMIK AIKAKYDVLI SIDTYKTETA RAALEAGADI LNDVRAGLYD
     GEMLALAAEY DVPIILMHNQ KEEVYQDVTQ DVCDFLSARA QAAIDAGVPK DNIWIDPGFG
     FPKSVQHNME LLKGLDHVCQ LGYPVLFGIS RKGVVDALLG GNTKAKERDG ATAALSAYAL
     GKGCQLVRVH DVKANQEIVA VLSQLM