ID DHP2_ECOLX Reviewed; 271 AA. AC P0AC11; P19539; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 115. 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; OS Escherichia coli. OG Plasmid pGS05, Plasmid pGS03B, and Plasmid IncQ RSF1010. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC PLASMID=IncQ RSF1010, pGS03B, and pGS05; RX PubMed=3075438; DOI=10.1128/aac.32.11.1684; RA Raedstroem P., Swedberg G.; RT "RSF1010 and a conjugative plasmid contain sulII, one of two known genes RT for plasmid-borne sulfonamide resistance dihydropteroate synthase."; RL Antimicrob. Agents Chemother. 32:1684-1692(1988). 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 (By similarity). It is implicated in resistance to sulfonamide. The CC type II enzyme is stable whereas type I DHPS loses its activity CC rapidly. {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 -!- MISCELLANEOUS: The sulII gene is located on various IncQ (Broad-host- CC range) plasmids and other small non-conjugative resistance plasmids. 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; M36657; AAA24936.1; -; Genomic_DNA. DR PIR; A34950; A34950. DR RefSeq; NP_957531.1; NC_005324.1. DR RefSeq; WP_001043260.1; NZ_WVWF01000037.1. DR RefSeq; YP_002455756.1; NC_011795.1. DR RefSeq; YP_002891091.1; NC_012690.1. DR RefSeq; YP_002894395.1; NC_012692.1. DR RefSeq; YP_002995721.1; NC_012886.1. DR RefSeq; YP_006940094.1; NC_018995.1. DR RefSeq; YP_006952281.1; NC_019060.1. DR RefSeq; YP_006952747.1; NC_019065.1. DR RefSeq; YP_006952891.1; NC_019066.1. DR RefSeq; YP_006953258.1; NC_019070.1. DR RefSeq; YP_006953602.1; NC_019080.1. DR RefSeq; YP_007349479.1; NC_020086.1. DR RefSeq; YP_008574999.1; NC_022377.1. DR RefSeq; YP_009061414.1; NC_024978.1. DR RefSeq; YP_009061550.1; NC_024979.1. DR RefSeq; YP_009061670.1; NC_024980.1. DR RefSeq; YP_009068735.1; NC_025142.1. DR RefSeq; YP_009068851.1; NC_025143.1. DR RefSeq; YP_009069120.1; NC_025144.1. DR RefSeq; YP_009070858.1; NC_025176.1. DR RefSeq; YP_794145.1; NC_008490.1. DR RefSeq; YP_891140.1; NC_008597.1. DR PDB; 7S2J; X-ray; 1.85 A; A/B/C/D=1-271. DR PDB; 7S2K; X-ray; 1.74 A; A/B=1-271. DR PDBsum; 7S2J; -. DR PDBsum; 7S2K; -. DR AlphaFoldDB; P0AC11; -. DR SMR; P0AC11; -. DR GeneID; 84568452; -. DR OMA; YDQGATF; -. DR UniPathway; UPA00077; UER00156. 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:0046677; P:response to antibiotic; 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 3D-structure; Antibiotic resistance; Folate biosynthesis; Magnesium; KW Metal-binding; Plasmid; Transferase. FT CHAIN 1..271 FT /note="Dihydropteroate synthase type-2" FT /id="PRO_0000168203" 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 //