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P05382 (DHPS_STRPN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydropteroate synthase

Short name=DHPS
EC=2.5.1.15
Alternative name(s):
Dihydropteroate pyrophosphorylase
Gene names
Name:sulA
Ordered Locus Names:SP_0289
OrganismStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) [Complete proteome] [HAMAP]
Taxonomic identifier170187 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DHPS catalyzes the formation of the immediate precursor of folic acid. It is implicated in resistance to sulfonamide.

Catalytic activity

(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.

Cofactor

Binds 1 magnesium ion per subunit. Magnesium is required for activity, even if it interacts primarily with the substrate By similarity.

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.

Subunit structure

Homodimer or homotrimer.

Miscellaneous

The sequence shown here is that of sul-s (wild-type). The protein of the spontaneous mutation to sulfonamide resistance (sul-d) has an insert of 2 AA.

Sequence similarities

Belongs to the DHPS family.

Contains 1 pterin-binding domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314Dihydropteroate synthase
PRO_0000168230

Regions

Domain10 – 294285Pterin-binding
Region57 – 582Substrate binding By similarity

Sites

Metal binding171Magnesium By similarity
Binding site251Substrate By similarity
Binding site911Substrate By similarity
Binding site1101Substrate By similarity
Binding site2011Substrate By similarity
Binding site2371Substrate By similarity
Binding site2821Substrate By similarity
Binding site2841Substrate By similarity

Natural variations

Natural variant671E → EIE in mutant SUL-D.

Experimental info

Sequence conflict122 – 1232AY → PH in AAB63944. Ref.1
Sequence conflict1311K → Q in AAB63944. Ref.1
Sequence conflict1591T → A in AAB63944. Ref.1
Sequence conflict1631K → E in AAB63944. Ref.1
Sequence conflict1751D → E in AAB63944. Ref.1
Sequence conflict1781V → E in AAB63944. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P05382 [UniParc].

Last modified September 26, 2001. Version 2.
Checksum: F2F20D9A782083FB

FASTA31434,403
        10         20         30         40         50         60 
MSSKANHAKT VICGIINVTP DSFSDGGQFF ALEQALQQAR KLIAEGASML DIGGESTRPG 

        70         80         90        100        110        120 
SSYVEIEEEI QRVVPVIKAI RKESDVLISI DTWKSQVAEA ALAAGADLVN DITGLMGDEK 

       130        140        150        160        170        180 
MAYVVAEARA KVVIMFNPVM ARPQHPSSLI FPHFGFGQTF TEKELADFET LPIEDLMVAF 

       190        200        210        220        230        240 
FERALARAAE AGIAPENILL DPGIGFGLTK KENLLLLRDL DKLHQKGYPI FLGVSRKRFV 

       250        260        270        280        290        300 
INILEENGFE VNPETELGFR NRDTASAHVT SIAARQGVEV VRVHDVASHR MAVEIASAIR 

       310 
LADEAENLDL KQYK 

« Hide

References

« Hide 'large scale' references
[1]"Sulfonamide resistance in Streptococcus pneumoniae: DNA sequence of the gene encoding dihydropteroate synthase and characterization of the enzyme."
Lopez P., Espinosa M., Greenberg B., Lacks S.A.
J. Bacteriol. 169:4320-4326(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 772.
[2]"Complete genome sequence of a virulent isolate of Streptococcus pneumoniae."
Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L. expand/collapse author list , Lewis M.R., Radune D., Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.
Science 293:498-506(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-334 / TIGR4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U16156 Genomic DNA. Translation: AAB63944.1.
AE005672 Genomic DNA. Translation: AAK74467.1.
PIRA43661.
B95034.
B97905.
RefSeqNP_344827.1. NC_003028.3.

3D structure databases

ProteinModelPortalP05382.
SMRP05382. Positions 7-303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP05382. 3 interactions.
STRING170187.SP_0289.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK74467; AAK74467; SP_0289.
GeneID930100.
KEGGspn:SP_0289.
PATRIC19704915. VBIStrPne105772_0303.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0294.
HOGENOMHOG000217509.
KOK00796.
OMADMFYVAA.
OrthoDBEOG67T5P5.

Enzyme and pathway databases

BioCycSPNE170187:GHGN-295-MONOMER.
SABIO-RKP05382.
UniPathwayUPA00077; UER00156.

Family and domain databases

Gene3D3.20.20.20. 1 hit.
InterProIPR006390. DHP_synth.
IPR011005. Dihydropteroate_synth-like.
IPR000489. Pterin-binding.
[Graphical view]
PfamPF00809. Pterin_bind. 1 hit.
[Graphical view]
SUPFAMSSF51717. SSF51717. 1 hit.
TIGRFAMsTIGR01496. DHPS. 1 hit.
PROSITEPS00792. DHPS_1. 1 hit.
PS00793. DHPS_2. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHPS_STRPN
AccessionPrimary (citable) accession number: P05382
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: September 26, 2001
Last modified: June 11, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways