ID   DHPS_STAAW              Reviewed;         267 AA.
AC   Q8NXZ2;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Dihydropteroate synthase;
DE            Short=DHPS;
DE            EC=2.5.1.15;
DE   AltName: Full=Dihydropteroate pyrophosphorylase;
GN   Name=folP; OrderedLocusNames=MW0469;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DHPS family. {ECO:0000305}.
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DR   EMBL; BA000033; BAB94334.1; -; Genomic_DNA.
DR   RefSeq; WP_000167924.1; NC_003923.1.
DR   AlphaFoldDB; Q8NXZ2; -.
DR   SMR; Q8NXZ2; -.
DR   EnsemblBacteria; BAB94334; BAB94334; BAB94334.
DR   KEGG; sam:MW0469; -.
DR   HOGENOM; CLU_008023_0_2_9; -.
DR   OMA; FSIDTYH; -.
DR   UniPathway; UPA00077; UER00156.
DR   Proteomes; UP000000418; 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..267
FT                   /note="Dihydropteroate synthase"
FT                   /id="PRO_0000168226"
FT   DOMAIN          1..251
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WND1"
FT   BINDING         51
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         84
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         103
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         167
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         203
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         239..241
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
SQ   SEQUENCE   267 AA;  29523 MW;  DE091EF7EF736093 CRC64;
     MTKTKIMGIL NVTPDSFSDG GKFNNVESAI NRVKAMIDEG ADIIDVGGVS TRPGHEMVSL
     EEEMNRVLPV VEAIVGFDVK ISVDTFRSEV AEACLKLGVD MINDQWAGLY DHRMFQIVAK
     YDAEIILMHN GNGNRDEPVV EEMLTSLLAQ AHQAKIAGIP SNKIWLDPGI GFAKTRNEEA
     EVMARLDELV ATEYPVLLAT SRKRFTKEMM GYDTTPVERD EVTAATTAYG IMKGVRAVRV
     HNVELNAKLA KGIDFLKENE NARHNLS