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Q5HRP0 (DHPS_STAEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. 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·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
Ordered Locus Names:SERP0153
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length272 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

Sequence similarities

Belongs to the DHPS family.

Contains 1 pterin-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 272272Dihydropteroate synthase
PRO_0000168228

Regions

Domain1 – 251251Pterin-binding
Region51 – 522Substrate binding By similarity

Sites

Metal binding111Magnesium By similarity
Binding site191Substrate By similarity
Binding site891Substrate By similarity
Binding site1081Substrate By similarity
Binding site1721Substrate By similarity
Binding site2081Substrate By similarity
Binding site2441Substrate By similarity
Binding site2461Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HRP0 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 5A9CE9F3822019B4

FASTA27230,373
        10         20         30         40         50         60 
MIKTKIMGIL NVTPDSFSDG GQYHSVDQAV KRAKEMIDEG VDIIDVGGVS TRPGHKEVSH 

        70         80         90        100        110        120 
KEVSLKEEMN RVLPVVESIV KYDVQISVDT FRSEVAEACL KLGVSMINDQ WAGLFDSNMF 

       130        140        150        160        170        180 
NVVSQYGAEI VLMHNGDGHR DKPVVEEMLV SLLAQANKAE LAGIPHNKIW LDPGIGFAKT 

       190        200        210        220        230        240 
REEENEVMAR LDELVATEYP VLLATSRKRY IKEMMNQDSS PSDRDEATAA TTAYGIMKGV 

       250        260        270 
RGVRVHNVLL NTRLAQSMDF LKENEYERHH LS 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW53522.1.
RefSeqYP_187749.1. NC_002976.3.

3D structure databases

ProteinModelPortalQ5HRP0.
SMRQ5HRP0. Positions 3-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176279.SERP0153.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW53522; AAW53522; SERP0153.
GeneID3240535.
KEGGser:SERP0153.
PATRIC19611163. VBIStaEpi130894_0144.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0294.
HOGENOMHOG000217509.
KOK00796.
OMADCWISVD.
OrthoDBEOG67T5P5.

Enzyme and pathway databases

BioCycSEPI176279:GJJB-157-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...

Entry information

Entry nameDHPS_STAEQ
AccessionPrimary (citable) accession number: Q5HRP0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 65 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

PATHWAY comments

Index of metabolic and biosynthesis pathways