ID   DHP2_SHIFL              Reviewed;         271 AA.
AC   P0AC12; P19539;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Dihydropteroate synthase type-2;
DE            EC=2.5.1.15;
DE   AltName: Full=Dihydropteroate pyrophosphorylase type II;
DE   AltName: Full=Dihydropteroate synthase type II;
DE            Short=DHPS;
GN   Name=sulII; OrderedLocusNames=S2703;
OS   Shigella flexneri.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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:0000305}.
CC   -!- SIMILARITY: Belongs to the DHPS family. {ECO:0000305}.
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DR   EMBL; AE014073; AAP17863.1; -; Genomic_DNA.
DR   RefSeq; WP_001043260.1; NZ_WPGW01000178.1.
DR   AlphaFoldDB; P0AC12; -.
DR   SMR; P0AC12; -.
DR   GeneID; 84568452; -.
DR   KEGG; sfx:S2703; -.
DR   HOGENOM; CLU_008023_0_3_6; -.
DR   UniPathway; UPA00077; UER00156.
DR   Proteomes; UP000002673; 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; Transferase.
FT   CHAIN           1..271
FT                   /note="Dihydropteroate synthase type-2"
FT                   /id="PRO_0000168204"
FT   DOMAIN          1..259
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT   BINDING         12
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WND1"
FT   BINDING         85
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         104
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         174
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         213
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         247..249
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
SQ   SEQUENCE   271 AA;  28470 MW;  4B00E71A3F7970FB CRC64;
     MNKSLIIFGI VNITSDSFSD GGRYLAPDAA IAQARKLMAE GADVIDLGPA SSNPDAAPVS
     SDTEIARIAP VLDALKADGI PVSLDSYQPA TQAYALSRGV AYLNDIRGFP DAAFYPQLAK
     SSAKLVVMHS VQDGQADRRE APAGDIMDHI AAFFDARIAA LTGAGIKRNR LVLDPGMGFF
     LGAAPETSLS VLARFDELRL RFDLPVLLSV SRKSFLRALT GRGPGDVGAA TLAAELAAAA
     GGADFIRTHE PRPLRDGLAV LAALKETARI R
//