ID   DHP1_ECOLX              Reviewed;         279 AA.
AC   P0C002; P11744; Q79LJ7; Q93K51;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Dihydropteroate synthase type-1;
DE            EC=2.5.1.15;
DE   AltName: Full=Dihydropteroate pyrophosphorylase type I;
DE   AltName: Full=Dihydropteroate synthase type I;
DE            Short=DHPS;
GN   Name=sulI; Synonyms=sul1;
OS   Escherichia coli.
OG   Plasmid IncFII R100 (NR1), Plasmid IncW R388, Plasmid pLMO20,
OG   Plasmid pLMO27, Plasmid IncN R46, Plasmid pDGO100, Plasmid R6-5,
OG   Plasmid pDGO101, Plasmid IncFII NR79, Plasmid IncW pSa,
OG   Plasmid IncP-beta R751, Plasmid pCMXR1, Plasmid pMSP071, Plasmid p1658/97,
OG   Plasmid pHSH1, Plasmid pHSH2, Plasmid pAK33, Plasmid p541, Plasmid pQR-1,
OG   Plasmid pKO56, Plasmid pKO97, and Plasmid pAPEC-O2-R.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=IncW R388, and pLMO20; TRANSPOSON=Tn21;
RX   PubMed=3054482; DOI=10.1007/bf00339581;
RA   Sundstroem L., Radstroem P., Swedberg G., Skoeld O.;
RT   "Site-specific recombination promotes linkage between trimethoprim- and
RT   sulfonamide resistance genes. Sequence characterization of dhfrV and sulI
RT   and a recombination active locus of Tn21.";
RL   Mol. Gen. Genet. 213:191-201(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=IncFII R100 (NR1), IncN R46, and pDGO101;
RX   PubMed=2560119; DOI=10.1111/j.1365-2958.1989.tb00153.x;
RA   Stokes H.W., Hall R.M.;
RT   "A novel family of potentially mobile DNA elements encoding site-specific
RT   gene-integration functions: integrons.";
RL   Mol. Microbiol. 3:1669-1683(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=IncN R46;
RX   PubMed=2662140; DOI=10.1093/nar/17.11.4370;
RA   Guerineau F., Mullineaux P.M.;
RT   "Nucleotide sequence of the sulfonamide resistance gene from plasmid R46.";
RL   Nucleic Acids Res. 17:4370-4370(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=R6-5; TRANSPOSON=Tn21;
RA   Sundstroem L.;
RL   Submitted (NOV-1989) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=IncFII NR79; TRANSPOSON=Tn2424;
RX   PubMed=1314803; DOI=10.1128/jb.174.9.2891-2897.1992;
RA   Parent R., Roy P.H.;
RT   "The chloramphenicol acetyltransferase gene of Tn2424: a new breed of
RT   cat.";
RL   J. Bacteriol. 174:2891-2897(1992).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF
RP   120-279.
RC   PLASMID=IncW pSa, and pDGO100;
RX   PubMed=8378445; DOI=10.1006/plas.1993.1032;
RA   Stokes H.W., Tomaras C., Parsons Y., Hall R.M.;
RT   "The partial 3'-conserved segment duplications in the integrons In6 from
RT   pSa and In7 from pDGO100 have a common origin.";
RL   Plasmid 30:39-50(1993).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=IncW pSa;
RX   PubMed=7846147; DOI=10.1006/plas.1994.1059;
RA   Valentine C.R., Heinrich M.J., Chissoe S.L., Roe B.A.;
RT   "DNA sequence of direct repeats of the sulI gene of plasmid pSa.";
RL   Plasmid 32:222-227(1994).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TRANSPOSON=Tn21;
RX   PubMed=10477306; DOI=10.1128/mmbr.63.3.507-522.1999;
RA   Liebert C.A., Hall R.M., Summers A.O.;
RT   "Transposon Tn21, flagship of the floating genome.";
RL   Microbiol. Mol. Biol. Rev. 63:507-522(1999).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MG-1; PLASMID=IncP-beta R751; TRANSPOSON=Tn2000;
RX   PubMed=11114922; DOI=10.1128/jb.183.1.235-249.2001;
RA   Naas T., Mikami Y., Imai T., Poirel L., Nordmann P.;
RT   "Characterization of In53, a class 1 plasmid- and composite transposon-
RT   located integron of Escherichia coli which carries an unusual array of gene
RT   cassettes.";
RL   J. Bacteriol. 183:235-249(2001).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=IncW R388;
RA   Partridge S.R., Hall R.M.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HKYM68; PLASMID=pCMXR1;
RX   PubMed=12121914; DOI=10.1128/aac.46.8.2427-2434.2002;
RA   Doi Y., Shibata N., Shibayama K., Kamachi K., Kurokawa H., Yokoyama K.,
RA   Yagi T., Arakawa Y.;
RT   "Characterization of a novel plasmid-mediated cephalosporinase (CMY-9) and
RT   its genetic environment in an Escherichia coli clinical isolate.";
RL   Antimicrob. Agents Chemother. 46:2427-2434(2002).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=785-D; PLASMID=pMSP071;
RX   PubMed=12121950; DOI=10.1128/aac.46.8.2656-2661.2002;
RA   Sabate M., Navarro F., Miro E., Campoy S., Mirelis B., Barbe J., Prats G.;
RT   "Novel complex sul1-type integron in Escherichia coli carrying bla(CTX-M-
RT   9).";
RL   Antimicrob. Agents Chemother. 46:2656-2661(2002).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=p1658/97;
RA   Zienkiewicz M., Kern-Zdanowicz I., Golebiewski M., Ceglowski P.;
RT   "p1658/97 complete sequence.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [14]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pHSH1, and pHSH2;
RX   PubMed=12821475; DOI=10.1128/aac.47.7.2242-2248.2003;
RA   Wang M., Tran J.H., Jacoby G.A., Zhang Y., Wang F., Hooper D.C.;
RT   "Plasmid-mediated quinolone resistance in clinical isolates of Escherichia
RT   coli from Shanghai, China.";
RL   Antimicrob. Agents Chemother. 47:2242-2248(2003).
RN   [15]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12821505; DOI=10.1128/aac.47.7.2380-2381.2003;
RA   Dubois V., Arpin C., Quentin C., Texier-Maugein J., Poirel L., Nordmann P.;
RT   "Decreased susceptibility to cefepime in a clinical strain of Escherichia
RT   coli related to plasmid- and integron-encoded OXA-30 beta-lactamase.";
RL   Antimicrob. Agents Chemother. 47:2380-2381(2003).
RN   [16]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pAK33;
RX   PubMed=12900034; DOI=10.1016/s0378-1097(03)00510-x;
RA   Vourli S., Tzouvelekis L.S., Tzelepi E., Lebessi E., Legakis N.J.,
RA   Miriagou V.;
RT   "Characterization of In111, a class 1 integron that carries the extended-
RT   spectrum beta, -lactamase gene blaIBC-1.";
RL   FEMS Microbiol. Lett. 225:149-153(2003).
RN   [17]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=p541;
RX   PubMed=15273143; DOI=10.1128/aac.48.8.3172-3174.2004;
RA   Miriagou V., Tzouvelekis L.S., Villa L., Lebessi E., Vatopoulos A.C.,
RA   Carattoli A., Tzelepi E.;
RT   "CMY-13, a novel inducible cephalosporinase encoded by an Escherichia coli
RT   plasmid.";
RL   Antimicrob. Agents Chemother. 48:3172-3174(2004).
RN   [18]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=IncW pSa;
RA   Partridge S.R., Hall R.M., Stokes H.W.;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN   [19]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Loup; PLASMID=pQR-1;
RX   PubMed=15616277; DOI=10.1128/aac.49.1.71-76.2005;
RA   Mammeri H., Van De Loo M., Poirel L., Martinez-Martinez L., Nordmann P.;
RT   "Emergence of plasmid-mediated quinolone resistance in Escherichia coli in
RT   Europe.";
RL   Antimicrob. Agents Chemother. 49:71-76(2005).
RN   [20]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pKO56, and pKO97;
RX   PubMed=15917562; DOI=10.1128/aac.49.6.2522-2524.2005;
RA   Jeong J.-Y., Yoon H.J., Kim E.S., Lee Y., Choi S.-H., Kim N.J., Woo J.H.,
RA   Kim Y.S.;
RT   "Detection of qnr in clinical isolates of Escherichia coli from Korea.";
RL   Antimicrob. Agents Chemother. 49:2522-2524(2005).
RN   [21]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A2363; PLASMID=pAPEC-O2-R;
RA   Johnson T.J., Nolan L.K.;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [22]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-120.
RC   PLASMID=pLMO27; TRANSPOSON=Tn5086;
RA   Sundstroem L., Swedberg G., Skoeld O.;
RL   Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases.
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 or homotrimer.
CC   -!- MISCELLANEOUS: The sulI gene is located on various large self-
CC       transmissible resistance plasmids and on transposons related to Tn21.
CC   -!- MISCELLANEOUS: The plasmid pDGO100 contains two copies of the sulI
CC       gene.
CC   -!- SIMILARITY: Belongs to the DHPS family. {ECO:0000305}.
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DR   EMBL; X12868; CAA31358.1; -; Genomic_DNA.
DR   EMBL; M95287; AAB59087.1; -; Genomic_DNA.
DR   EMBL; U42226; AAC53726.1; -; Genomic_DNA.
DR   EMBL; X15024; CAA33123.1; -; Genomic_DNA.
DR   EMBL; A07921; CAA00729.1; -; Unassigned_DNA.
DR   EMBL; X12870; CAA31364.1; -; Genomic_DNA.
DR   EMBL; AF047479; AAC14739.1; -; Genomic_DNA.
DR   EMBL; L06418; AAA92747.1; -; Genomic_DNA.
DR   EMBL; L06418; AAA92751.3; -; Genomic_DNA.
DR   EMBL; U04277; AAB60179.1; -; Genomic_DNA.
DR   EMBL; AF071413; AAC33914.1; -; Genomic_DNA.
DR   EMBL; AF205943; AAG45723.1; -; Genomic_DNA.
DR   EMBL; U12441; AAK95985.1; -; Genomic_DNA.
DR   EMBL; AB061794; BAB72156.1; -; Genomic_DNA.
DR   EMBL; AF174129; AAK60189.2; -; Genomic_DNA.
DR   EMBL; AF550679; AAO49595.1; -; Genomic_DNA.
DR   EMBL; AY259085; AAP20908.1; -; Genomic_DNA.
DR   EMBL; AY259085; AAP20913.1; -; Genomic_DNA.
DR   EMBL; AY259086; AAP20924.1; -; Genomic_DNA.
DR   EMBL; AY259086; AAP20929.1; -; Genomic_DNA.
DR   EMBL; AY224185; AAP51287.1; -; Genomic_DNA.
DR   EMBL; AY260546; AAP22979.1; -; Genomic_DNA.
DR   EMBL; AY339625; AAQ16671.1; -; Genomic_DNA.
DR   EMBL; L06822; AAW29415.1; -; Genomic_DNA.
DR   EMBL; L06822; AAW29418.1; -; Genomic_DNA.
DR   EMBL; AY655485; AAW31097.1; -; Genomic_DNA.
DR   EMBL; AY878717; AAX18266.1; -; Genomic_DNA.
DR   EMBL; AY878717; AAX18269.1; -; Genomic_DNA.
DR   EMBL; AY878718; AAX18276.1; -; Genomic_DNA.
DR   EMBL; AY878718; AAX18279.1; -; Genomic_DNA.
DR   EMBL; AY214164; AAP51280.1; -; Genomic_DNA.
DR   EMBL; X58425; CAA41328.1; -; Genomic_DNA.
DR   PIR; A60174; SYECOG.
DR   PIR; T45123; T45123.
DR   RefSeq; NP_863000.1; NC_004998.1.
DR   RefSeq; WP_000259031.1; NZ_WXZA01000039.1.
DR   RefSeq; YP_001096354.1; NC_009132.1.
DR   RefSeq; YP_001096411.1; NC_009133.1.
DR   RefSeq; YP_002891164.1; NC_012690.1.
DR   RefSeq; YP_002894492.1; NC_012692.1.
DR   RefSeq; YP_004558213.1; NC_015599.1.
DR   RefSeq; YP_006903340.1; NC_019045.2.
DR   RefSeq; YP_006939957.1; NC_018994.1.
DR   RefSeq; YP_006952407.1; NC_019062.1.
DR   RefSeq; YP_006952437.1; NC_019063.1.
DR   RefSeq; YP_006952978.1; NC_019066.1.
DR   RefSeq; YP_006953197.1; NC_019069.1.
DR   RefSeq; YP_006953612.1; NC_019081.1.
DR   RefSeq; YP_006953620.1; NC_019082.1.
DR   RefSeq; YP_008574825.1; NC_022374.1.
DR   RefSeq; YP_009023104.1; NC_023909.1.
DR   RefSeq; YP_009060115.1; NC_024956.1.
DR   RefSeq; YP_009061085.1; NC_024975.1.
DR   RefSeq; YP_009068292.1; NC_025139.1.
DR   RefSeq; YP_009070794.1; NC_025175.1.
DR   RefSeq; YP_009182147.1; NC_028464.1.
DR   RefSeq; YP_190215.1; NC_006671.1.
DR   RefSeq; YP_724471.1; NC_007682.3.
DR   PDB; 7S2I; X-ray; 2.32 A; A/B=1-279.
DR   PDBsum; 7S2I; -.
DR   AlphaFoldDB; P0C002; -.
DR   SMR; P0C002; -.
DR   DrugBank; DB00634; Sulfacetamide.
DR   GeneID; 84690159; -.
DR   OMA; YIMKNID; -.
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; Transposable element.
FT   CHAIN           1..279
FT                   /note="Dihydropteroate synthase type-1"
FT                   /id="PRO_0000168201"
FT   DOMAIN          1..258
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WND1"
FT   BINDING         82
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         101
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         173
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         246..248
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   CONFLICT        259
FT                   /note="F -> I (in Ref. 3; CAA00729)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   279 AA;  30126 MW;  13EE36C6E3FBDF63 CRC64;
     MVTVFGILNL TEDSFFDESR RLDPAGAVTA AIEMLRVGSD VVDVGPAASH PDARPVSPAD
     EIRRIAPLLD ALSDQMHRVS IDSFQPETQR YALKRGVGYL NDIQGFPDPA LYPDIAEADC
     RLVVMHSAQR DGIATRTGHL RPEDALDEIV RFFEARVSAL RRSGVAADRL ILDPGMGFFL
     SPAPETSLHV LSNLQKLKSA LGLPLLVSVS RKSFLGATVG LPVKDLGPAS LAAELHAIGN
     GADYVRTHAP GDLRSAITFS ETLAKFRSRD ARDRGLDHA
//