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P59655 (DHPS_STRR6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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:spr0266
OrganismStreptococcus pneumoniae (strain ATCC BAA-255 / R6) [Reference proteome] [HAMAP]
Taxonomic identifier171101 [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. Ref.2

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. Ref.2

Sequence similarities

Belongs to the DHPS family.

Contains 1 pterin-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314Dihydropteroate synthase
PRO_0000168231

Regions

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

Sites

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

Secondary structure

.............................................. 314
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P59655 [UniParc].

Last modified April 30, 2003. Version 1.
Checksum: C7CEDD0C2EDAA061

FASTA31434,418
        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 
MPHVVAEARA QVVIMFNPVM ARPQHPSSLI FPHFGFGQAF TEEELADFET LPIEELMEAF 

       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]"Genome of the bacterium Streptococcus pneumoniae strain R6."
Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J., Lee L.N. expand/collapse author list , Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M., McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B., Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y., Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R., Rosteck P.R. Jr., Skatrud P.L., Glass J.I.
J. Bacteriol. 183:5709-5717(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-255 / R6.
[2]"Dihydropteroate synthase from Streptococcus pneumoniae: structure, ligand recognition and mechanism of sulfonamide resistance."
Levy C., Minnis D., Derrick J.P.
Biochem. J. 412:379-388(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH PTERIN-6-YL-METHYL-MONOPHOSPHATE, SUBUNIT, FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE007317 Genomic DNA. Translation: AAK99070.1.
RefSeqNP_357860.1. NC_003098.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VEFX-ray1.80A/B1-314[»]
2VEGX-ray2.40A/B1-314[»]
ProteinModelPortalP59655.
SMRP59655. Positions 7-303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING171101.spr0266.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK99070; AAK99070; spr0266.
GeneID934662.
KEGGspr:spr0266.
PATRIC19700365. VBIStrPne107296_0303.

Phylogenomic databases

eggNOGCOG0294.
HOGENOMHOG000217509.
KOK00796.
OMASALAGWH.
OrthoDBEOG67T5P5.

Enzyme and pathway databases

BioCycSPNE171101:GJC8-273-MONOMER.
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...

Other

EvolutionaryTraceP59655.

Entry information

Entry nameDHPS_STRR6
AccessionPrimary (citable) accession number: P59655
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: May 14, 2014
This is version 75 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways