ID   DHPS_STAAN              Reviewed;         267 AA.
AC   P64142; Q99W89;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Dihydropteroate synthase;
DE            Short=DHPS;
DE            EC=2.5.1.15;
DE   AltName: Full=Dihydropteroate pyrophosphorylase;
GN   Name=folP; OrderedLocusNames=SA0472;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000018; BAB41702.1; -; Genomic_DNA.
DR   PIR; C89818; C89818.
DR   RefSeq; WP_000167944.1; NC_002745.2.
DR   AlphaFoldDB; P64142; -.
DR   SMR; P64142; -.
DR   PRIDE; P64142; -.
DR   EnsemblBacteria; BAB41702; BAB41702; BAB41702.
DR   KEGG; sau:SA0472; -.
DR   HOGENOM; CLU_008023_0_2_9; -.
DR   OMA; FSIDTYH; -.
DR   UniPathway; UPA00077; UER00156.
DR   Proteomes; UP000000751; 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_0000168222"
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;  29533 MW;  A2E41F5C5544D86C CRC64;
     MTKTKIMGIL NVTPDSFSDG GKFNNVETAI NRVKAMIDEG ADIIDVGGVS TRPGHEMVTL
     EEELNRVLPV VEAIVGFDVK ISVDTFRSEV AEACLKLGVD MINDQWAGLY DHRMFQIVAK
     YDAEIILMHN GNGNRDEPVV EEMLTSLLAQ AHQAKIAGIP SNKIWLDPGI GFAKTRNEEA
     EVMARLDELV ATEYPVLLAT SRKRFTKEMM GYDTTPVERD EVTAATTAYG IMKGVRAVRV
     HNVELNAKLA KGIDFLKENE NARHNLS