ID   DHP1_MYCFO              Reviewed;         283 AA.
AC   Q49184;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=suf3;
OS   Mycolicibacterium fortuitum (Mycobacterium fortuitum).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1766;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INVOLVEMENT IN RESISTANCE TO
RP   SULFONAMIDE.
RC   STRAIN=FC1; TRANSPOSON=Tn610;
RX   PubMed=2163027; DOI=10.1038/345739a0;
RA   Martin C., Timm J., Rauzier J., Gomez-Lus R., Davies J., Gicquel B.;
RT   "Transposition of an antibiotic resistance element in mycobacteria.";
RL   Nature 345:739-743(1990).
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). Implicated in resistance to sulfonamide
CC       (PubMed:2163027). {ECO:0000250|UniProtKB:P0AC13,
CC       ECO:0000269|PubMed:2163027}.
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. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The sulI gene is located on various large self-
CC       transmissible resistance plasmids and on transposons related to Tn21.
CC   -!- SIMILARITY: Belongs to the DHPS family. {ECO:0000305}.
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DR   EMBL; X53635; CAA37684.1; -; Genomic_DNA.
DR   PIR; S10928; S10928.
DR   AlphaFoldDB; Q49184; -.
DR   SMR; Q49184; -.
DR   DrugBank; DB00891; Sulfapyridine.
DR   DrugCentral; Q49184; -.
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   Transferase; Transposable element.
FT   CHAIN           1..283
FT                   /note="Dihydropteroate synthase type-1"
FT                   /id="PRO_0000321868"
FT   DOMAIN          6..262
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WND1"
FT   BINDING         86
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         105
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         177
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         216
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
FT   BINDING         250..252
FT                   /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:72950"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC13"
SQ   SEQUENCE   283 AA;  30639 MW;  F04DB17FB1A4951E CRC64;
     MLRSRVTVFG ILNLTEDSFF DESRRLDPAG AVTAAIEMLR VGSDVVDVGP AASHPDARPV
     SPADEIRRIA PLLDALSDQM HRVSIDSFQP ETQRYALKRG VGYLNDIQGF PDPALYPDIA
     EADCRLVVMH SAQRDGIATR TGHLRPEDAL DEIVRFFEAR VSALRRSGVA ADRLILDPGM
     GFFLSPAPET SLHVLSNLQK LKSALGLPLL VSVSRKSFLG ATVGLPVKDL GPASLAAELH
     AIGNGADYVR THAPGDLRSA ITFSETLAKF RSRDARDRGL DHA