DHP1_ECOLX
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 03-AUG-2022, entry version 110.
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; Proteobacteria; 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_WWEL01000045.1.
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_003937681.1; NC_014615.1.
DR RefSeq; YP_004558213.1; NC_015599.1.
DR RefSeq; YP_006902980.1; NC_019037.1.
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 AlphaFoldDB; P0C002; -.
DR SMR; P0C002; -.
DR DrugBank; DB00634; Sulfacetamide.
DR GeneID; 67375551; -.
DR OMA; YIMKNID; -.
DR OrthoDB; 1275854at2; -.
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; -; 1.
DR InterPro; IPR045031; DHP_synth.
DR InterPro; IPR006390; DHP_synth_dom.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
DR InterPro; IPR000489; Pterin-binding_dom.
DR PANTHER; PTHR20941; PTHR20941; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF51717; SSF51717; 1.
DR TIGRFAMs; TIGR01496; DHPS; 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 Antibiotic resistance; Folate biosynthesis; Magnesium; Metal-binding;
KW 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
