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O05701 (DHPS_STAAU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 80. 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:folP
OrganismStaphylococcus aureus
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length267 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.1

Catalytic activity

(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate. Ref.1

Cofactor

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

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.1

Sequence similarities

Belongs to the DHPS family.

Contains 1 pterin-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 267267Dihydropteroate synthase
PRO_0000168225

Regions

Domain1 – 251251Pterin-binding
Region51 – 522Substrate binding

Sites

Metal binding111Magnesium
Binding site191Substrate
Binding site841Substrate
Binding site1031Substrate
Binding site1671Substrate
Binding site2031Substrate
Binding site2391Substrate
Binding site2411Substrate

Secondary structure

.............................................. 267
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O05701 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: F9FB01B1EAFBC275

FASTA26729,498
        10         20         30         40         50         60 
MTKTKIMGIL NVTPDSFSDG GKFNNVESAV TRVKAMMDEG ADIIDVGGVS TRPGHEMITV 

        70         80         90        100        110        120 
EEELNRVLPV VEAIVGFDVK ISVDTFRSEV AEACLKLGVD IINDQWAGLY DHRMFQVVAK 

       130        140        150        160        170        180 
YDAEIVLMHN GNGNRDEPVV EEMLTSLLAQ AHQAKIAGIP SNKIWLDPGI GFAKTRNEEA 

       190        200        210        220        230        240 
EVMARLDELV ATEYPVLLAT SRKRFTKEMM GYDTTPVERD EVTAATTAYG IMKGVRAVRV 

       250        260 
HNVELNAKLA KGIDFLKENE NARHNFS 

« Hide

References

[1]"Structure and function of the dihydropteroate synthase from Staphylococcus aureus."
Hampele I.C., D'Arcy A., Dale G.E., Kostrewa D., Nielsen J., Oefner C., Page M.G.P., Schoenfeld H.-J., Stueber D., Then R.L.
J. Mol. Biol. 268:21-30(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS; HYDROXYMETHYLPTERIN PYROPHOSPHATE, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY.
Strain: ATCC 25923 / DSM 1104 / Seattle 1945 / FO 14462 / JCM 2413.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z84573 Genomic DNA. Translation: CAB06539.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AD1X-ray2.20A/B2-267[»]
1AD4X-ray2.40A/B2-267[»]
ProteinModelPortalO05701.
SMRO05701. Positions 2-265.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0294.

Enzyme and pathway databases

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

EvolutionaryTraceO05701.

Entry information

Entry nameDHPS_STAAU
AccessionPrimary (citable) accession number: O05701
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: October 16, 2013
This is version 80 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