ID DHPS_STRP1 Reviewed; 266 AA. AC P0C0G1; O33724; Q48YY2; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 123. DE RecName: Full=Dihydropteroate synthase; DE Short=DHPS; DE EC=2.5.1.15; DE AltName: Full=Dihydropteroate pyrophosphorylase; GN Name=folP; OrderedLocusNames=SPy_1098, M5005_Spy0822; OS Streptococcus pyogenes serotype M1. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=301447; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700294 / SF370 / Serotype M1; RX PubMed=11296296; DOI=10.1073/pnas.071559398; RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K., RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P., RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X., RA Clifton S.W., Roe B.A., McLaughlin R.E.; RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes."; RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1; RX PubMed=16088826; DOI=10.1086/432514; RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K., RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P., RA Musser J.M.; RT "Evolutionary origin and emergence of a highly successful clone of serotype RT M1 group A Streptococcus involved multiple horizontal gene transfer RT events."; RL J. Infect. Dis. 192:771-782(2005). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE004092; AAK33976.1; -; Genomic_DNA. DR EMBL; CP000017; AAZ51440.1; -; Genomic_DNA. DR RefSeq; NP_269255.1; NC_002737.2. DR AlphaFoldDB; P0C0G1; -. DR SMR; P0C0G1; -. DR PaxDb; 1314-HKU360_00887; -. DR KEGG; spy:SPy_1098; -. DR KEGG; spz:M5005_Spy0822; -. DR PATRIC; fig|160490.10.peg.954; -. DR HOGENOM; CLU_008023_0_2_9; -. DR OMA; FATPRDC; -. DR SABIO-RK; P0C0G1; -. DR UniPathway; UPA00077; UER00156. DR Proteomes; UP000000750; 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 3: Inferred from homology; KW Folate biosynthesis; Magnesium; Metal-binding; Reference proteome; KW Transferase. FT CHAIN 1..266 FT /note="Dihydropteroate synthase" FT /id="PRO_0000168233" 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; 28642 MW; B04D0C553B5BAB22 CRC64; MKIGKFVIEG NAAIMGILNV TPDSFSDGGS YTTVQKALDH VEQMIADGAK IIDVGGESTR PGCQFVSATD EIDRVVPVIK AIKENYDILI SIDTYKTETA RAALEAGADI LNDVWAGLYD GQMFALAAEY DAPIILMHNQ DEEVYQEVTQ DVCDFLGNRA QAALDAGVPK NNIWVDPGFG FAKSVQQNTE LLKGLDRVCQ LGYPVLFGIS RKRVVDALLG GNTKAKERDG ATAALSAYAL GKGCQIVRVH DVKANQDIVA VLSQLM //