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P57696 (DHPS_NEIMC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Synonyms:dhpS
OrganismNeisseria meningitidis serogroup C
Taxonomic identifier135720 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length283 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.

Sequence similarities

Belongs to the DHPS family.

Contains 1 pterin-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 283283Dihydropteroate synthase
PRO_0000168219

Regions

Domain18 – 274257Pterin-binding
Region66 – 672Substrate binding By similarity

Sites

Metal binding251Magnesium By similarity
Binding site331Substrate By similarity
Binding site991Substrate By similarity
Binding site1191Substrate By similarity
Binding site1901Substrate By similarity
Binding site2271Substrate By similarity
Binding site2621Substrate By similarity
Binding site2641Substrate By similarity

Natural variations

Natural variant361V → A in strain: BT054.
Natural variant42 – 432QT → RI in strain: BT054.
Natural variant501Q → R in strain: BT054.
Natural variant681S → P in strain: BT054.
Natural variant961I → V in strain: BT054.
Natural variant104 – 1052VI → AV in strain: BT054.
Natural variant1071E → G in strain: BT054.
Natural variant1251N → T in strain: BT054.
Natural variant1371A → T in strain: BT054.
Natural variant1511K → E in strain: BT054.
Natural variant1521N → T in strain: MO124.
Natural variant1741A → S in strain: MO124.
Natural variant1781I → V in strain: BT054.
Natural variant1881T → I in strain: MO124.
Natural variant1941C → G in strain: BT054.
Natural variant1941C → GSG in strain: MO124.
Natural variant1981T → P in strain: MO124.
Natural variant2041T → A in strain: BT054 and MO124.
Natural variant2181Y → F in strain: BT054 and MO124.
Natural variant2281S → R in strain: BT054.
Natural variant2291M → T in strain: MO124.
Natural variant2301I → V in strain: BT054.
Natural variant237 – 2382TD → AN in strain: MO124.
Natural variant2411A → E in strain: MO124.
Natural variant2431G → V in strain: BT054 and MO124.
Natural variant2531A → S in strain: BT054 and MO124.
Natural variant2591K → Q in strain: BT054 and MO124.
Natural variant2751A → V in strain: BT054 and MO124.

Sequences

Sequence LengthMass (Da)Tools
P57696 [UniParc].

Last modified September 26, 2001. Version 2.
Checksum: FE8D19EFA15FA034

FASTA28330,167
        10         20         30         40         50         60 
MARHVWQAGR FEIGLDKPKI MGIVNLTPDS FSDGGVYSQN AQTALAHAEQ LLKEGADILD 

        70         80         90        100        110        120 
IGGESTRSGA DYVSPEEEWA RVEPVLAEVA GWGVPISLDT RRTVIMEKAL ALGGIDIIND 

       130        140        150        160        170        180 
VAALNDEGAV ELLARQADTG ICLMHMQGLP KNMQINPKYQ DVVGEVARYL KARAAECIAA 

       190        200        210        220        230        240 
GIAPQRITLD PGFCFGKTLQ HNITLMRHLP ELMAETGYPL LIGVSRKSMI GELTGETDAA 

       250        260        270        280 
ARGHGSVAAA LAAVARGAKI VRVHDVKATA DALKAWEALG INL 

« Hide

References

[1]"Transformational exchanges in the dihydropteroate synthase gene of Neisseria meningitidis: a novel mechanism for acquisition of sulfonamide resistance."
Raadstroem P., Fermer C., Kristiansen B.-E., Jenkins A., Skoeld O., Swedberg G.
J. Bacteriol. 174:6386-6393(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BT054 / Serogroup C / Serotype 15, BT227 / Serogroup C / Serotype 2a and CCUG 23102 / MO124 / Serogroup C / Serotype 15.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68063 Genomic DNA. Translation: CAA48200.1.
X68067 Genomic DNA. Translation: CAA48204.1.
X68064 Genomic DNA. Translation: CAA48201.1.
PIRA57423.
S25612.

3D structure databases

ProteinModelPortalP57696.
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.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHPS_NEIMC
AccessionPrimary (citable) accession number: P57696
Entry history
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: September 26, 2001
Last modified: February 19, 2014
This is version 73 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