DHPS_STRPN
ID DHPS_STRPN Reviewed; 314 AA.
AC P05382;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Dihydropteroate synthase;
DE Short=DHPS;
DE EC=2.5.1.15;
DE AltName: Full=Dihydropteroate pyrophosphorylase;
GN Name=sulA; OrderedLocusNames=SP_0289;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=772;
RX PubMed=3114239; DOI=10.1128/jb.169.9.4320-4326.1987;
RA Lopez P., Espinosa M., Greenberg B., Lacks S.A.;
RT "Sulfonamide resistance in Streptococcus pneumoniae: DNA sequence of the
RT gene encoding dihydropteroate synthase and characterization of the
RT enzyme.";
RL J. Bacteriol. 169:4320-4326(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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 {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 -!- INTERACTION:
CC P05382; Q97NV3: groES; NbExp=2; IntAct=EBI-2206997, EBI-2206949;
CC P05382; P0A4T1: malR; NbExp=2; IntAct=EBI-2206997, EBI-2207435;
CC P05382; A0A0H2UPV6: SP_1069; NbExp=4; IntAct=EBI-2206997, EBI-6472250;
CC -!- MISCELLANEOUS: The sequence shown here is that of sul-s (wild-type).
CC The protein of the spontaneous mutation to sulfonamide resistance (sul-
CC d) has an insert of 2 AA.
CC -!- SIMILARITY: Belongs to the DHPS family. {ECO:0000305}.
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DR EMBL; U16156; AAB63944.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK74467.1; -; Genomic_DNA.
DR PIR; A43661; A43661.
DR PIR; B95034; B95034.
DR PIR; B97905; B97905.
DR AlphaFoldDB; P05382; -.
DR SMR; P05382; -.
DR IntAct; P05382; 3.
DR STRING; 170187.SP_0289; -.
DR EnsemblBacteria; AAK74467; AAK74467; SP_0289.
DR KEGG; spn:SP_0289; -.
DR eggNOG; COG0294; Bacteria.
DR OMA; FSIDTYH; -.
DR PhylomeDB; P05382; -.
DR BioCyc; SPNE170187:G1FZB-298-MON; -.
DR SABIO-RK; P05382; -.
DR UniPathway; UPA00077; UER00156.
DR Proteomes; UP000000585; Chromosome.
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: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 1: Evidence at protein level;
KW Folate biosynthesis; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..314
FT /note="Dihydropteroate synthase"
FT /id="PRO_0000168230"
FT DOMAIN 10..294
FT /note="Pterin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WND1"
FT BINDING 57
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 91
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 110
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 201
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 237
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 282..284
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT VARIANT 67
FT /note="E -> EIE (in mutant SUL-D)"
FT CONFLICT 122..123
FT /note="AY -> PH (in Ref. 1; AAB63944)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="K -> Q (in Ref. 1; AAB63944)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="T -> A (in Ref. 1; AAB63944)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="K -> E (in Ref. 1; AAB63944)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="D -> E (in Ref. 1; AAB63944)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="V -> E (in Ref. 1; AAB63944)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 34403 MW; F2F20D9A782083FB CRC64;
MSSKANHAKT VICGIINVTP DSFSDGGQFF ALEQALQQAR KLIAEGASML DIGGESTRPG
SSYVEIEEEI QRVVPVIKAI RKESDVLISI DTWKSQVAEA ALAAGADLVN DITGLMGDEK
MAYVVAEARA KVVIMFNPVM ARPQHPSSLI FPHFGFGQTF TEKELADFET LPIEDLMVAF
FERALARAAE AGIAPENILL DPGIGFGLTK KENLLLLRDL DKLHQKGYPI FLGVSRKRFV
INILEENGFE VNPETELGFR NRDTASAHVT SIAARQGVEV VRVHDVASHR MAVEIASAIR
LADEAENLDL KQYK
