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Q59919 (DHPS_STAHA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 70. 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
OrganismStaphylococcus haemolyticus
Taxonomic identifier1283 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length267 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.

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_0000168229

Regions

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

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q59919 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 87807DFB3FBA8CBD

FASTA26729,613
        10         20         30         40         50         60 
MTKTKIIGIL NVTPDSFSDG GKYNSVDKAI ARAKEMIDEG VDIIDVGGVS TRPGHTEVSL 

        70         80         90        100        110        120 
EEEMERVVPV VEQLVKLDVQ ISVDTYRSEV AEACLKLGAT MINDQWAGLY DPKIFDVVSD 

       130        140        150        160        170        180 
YNAEIVLMHN GDGQREQPVV EEMLLSLLTQ ANKAEMAGIE KGNIWLDPGI GFAKSRSEEK 

       190        200        210        220        230        240 
EVMARLDELV ATEYPVLLAT SRKRFIKEMI GKETTPAERD EATAATTVYG IMKGIQAVRV 

       250        260 
HNVDLNVKLA QSIDFLKENE HERHHLS 

« Hide

References

[1]"Functional cloning of the dihydropteroate synthase gene of Staphylococcus haemolyticus."
Kellam P., Dallas W.S., Ballantine S.P., Delves C.J.
FEMS Microbiol. Lett. 134:165-169(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U40768 Genomic DNA. Translation: AAC43583.1.

3D structure databases

ProteinModelPortalQ59919.
SMRQ59919. Positions 2-265.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Entry information

Entry nameDHPS_STAHA
AccessionPrimary (citable) accession number: Q59919
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 70 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