DHP2_ECOLX
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 03-AUG-2022, entry version 107.
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; Proteobacteria; 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}.
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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 AlphaFoldDB; P0AC11; -.
DR SMR; P0AC11; -.
DR GeneID; 64223951; -.
DR GeneID; 66976586; -.
DR OMA; EAPMNKS; -.
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.
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
