ID   DHPS_STRPN              Reviewed;         314 AA.
AC   P05382;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=Dihydropteroate synthase;
DE            Short=DHPS;
DE            EC=2.5.1.15;
DE   AltName: Full=Dihydropteroate pyrophosphorylase;
GN   Name=sulA; OrderedLocusNames=SP_0289;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=772;
RX   PubMed=3114239; DOI=10.1128/jb.169.9.4320-4326.1987;
RA   Lopez P., Espinosa M., Greenberg B., Lacks S.A.;
RT   "Sulfonamide resistance in Streptococcus pneumoniae: DNA sequence of the
RT   gene encoding dihydropteroate synthase and characterization of the
RT   enzyme.";
RL   J. Bacteriol. 169:4320-4326(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(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 or homotrimer.
CC   -!- INTERACTION:
CC       P05382; Q97NV3: groES; NbExp=2; IntAct=EBI-2206997, EBI-2206949;
CC       P05382; P0A4T1: malR; NbExp=2; IntAct=EBI-2206997, EBI-2207435;
CC       P05382; A0A0H2UPV6: SP_1069; NbExp=4; IntAct=EBI-2206997, EBI-6472250;
CC   -!- MISCELLANEOUS: The sequence shown here is that of sul-s (wild-type).
CC       The protein of the spontaneous mutation to sulfonamide resistance (sul-
CC       d) has an insert of 2 AA.
CC   -!- SIMILARITY: Belongs to the DHPS family. {ECO:0000305}.
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DR   EMBL; U16156; AAB63944.1; -; Genomic_DNA.
DR   EMBL; AE005672; AAK74467.1; -; Genomic_DNA.
DR   PIR; A43661; A43661.
DR   PIR; B95034; B95034.
DR   PIR; B97905; B97905.
DR   AlphaFoldDB; P05382; -.
DR   SMR; P05382; -.
DR   IntAct; P05382; 3.
DR   PaxDb; 170187-SP_0289; -.
DR   EnsemblBacteria; AAK74467; AAK74467; SP_0289.
DR   KEGG; spn:SP_0289; -.
DR   eggNOG; COG0294; Bacteria.
DR   PhylomeDB; P05382; -.
DR   BioCyc; SPNE170187:G1FZB-298-MONOMER; -.
DR   SABIO-RK; P05382; -.
DR   UniPathway; UPA00077; UER00156.
DR   Proteomes; UP000000585; 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; Dihydropteroate synthase-like; 1.
DR   InterPro; IPR045031; DHP_synth-like.
DR   InterPro; IPR006390; DHP_synth_dom.
DR   InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR   InterPro; IPR000489; Pterin-binding_dom.
DR   NCBIfam; TIGR01496; DHPS; 1.
DR   PANTHER; PTHR20941; FOLATE SYNTHESIS PROTEINS; 1.
DR   PANTHER; PTHR20941:SF1; FOLIC ACID SYNTHESIS PROTEIN FOL1; 1.
DR   Pfam; PF00809; Pterin_bind; 1.
DR   SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR   PROSITE; PS00792; DHPS_1; 1.
DR   PROSITE; PS00793; DHPS_2; 1.
DR   PROSITE; PS50972; PTERIN_BINDING; 1.
PE   1: Evidence at protein level;
KW   Folate biosynthesis; Magnesium; Metal-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..314
FT                   /note="Dihydropteroate synthase"
FT                   /id="PRO_0000168230"
FT   DOMAIN          10..294
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT   BINDING         17
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WND1"
FT   BINDING         57
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         91
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         110
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         201
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         237
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         282..284
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   VARIANT         67
FT                   /note="E -> EIE (in mutant SUL-D)"
FT   CONFLICT        122..123
FT                   /note="AY -> PH (in Ref. 1; AAB63944)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        131
FT                   /note="K -> Q (in Ref. 1; AAB63944)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        159
FT                   /note="T -> A (in Ref. 1; AAB63944)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="K -> E (in Ref. 1; AAB63944)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        175
FT                   /note="D -> E (in Ref. 1; AAB63944)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        178
FT                   /note="V -> E (in Ref. 1; AAB63944)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   314 AA;  34403 MW;  F2F20D9A782083FB CRC64;
     MSSKANHAKT VICGIINVTP DSFSDGGQFF ALEQALQQAR KLIAEGASML DIGGESTRPG
     SSYVEIEEEI QRVVPVIKAI RKESDVLISI DTWKSQVAEA ALAAGADLVN DITGLMGDEK
     MAYVVAEARA KVVIMFNPVM ARPQHPSSLI FPHFGFGQTF TEKELADFET LPIEDLMVAF
     FERALARAAE AGIAPENILL DPGIGFGLTK KENLLLLRDL DKLHQKGYPI FLGVSRKRFV
     INILEENGFE VNPETELGFR NRDTASAHVT SIAARQGVEV VRVHDVASHR MAVEIASAIR
     LADEAENLDL KQYK
//