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P0AC13 (DHPS_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
Synonyms:dhpS
Ordered Locus Names:b3177, JW3144
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length282 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.7

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit. Magnesium is required for activity, even if it interacts primarily with the substrate. Ref.7

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.8

Sequence similarities

Belongs to the DHPS family.

Contains 1 pterin-binding domain.

Sequence caution

The sequence AAA57978.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 282282Dihydropteroate synthase
PRO_0000168207

Regions

Domain15 – 267253Pterin-binding
Region62 – 632Substrate binding

Sites

Metal binding221Magnesium
Binding site301Substrate
Binding site961Substrate
Binding site1151Substrate
Binding site1851Substrate
Binding site2211Substrate
Binding site2551Substrate
Binding site2571Substrate

Natural variations

Natural variant281F → I in TS20; resistant to sulfonamide and temperature-sensitive.

Experimental info

Sequence conflict61Q → E AA sequence Ref.6
Sequence conflict771R → A in AAA97509. Ref.3

Secondary structure

................................................. 282
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AC13 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 6230C8883796F59E

FASTA28230,615
        10         20         30         40         50         60 
MKLFAQGTSL DLSHPHVMGI LNVTPDSFSD GGTHNSLIDA VKHANLMINA GATIIDVGGE 

        70         80         90        100        110        120 
STRPGAAEVS VEEELQRVIP VVEAIAQRFE VWISVDTSKP EVIRESAKVG AHIINDIRSL 

       130        140        150        160        170        180 
SEPGALEAAA ETGLPVCLMH MQGNPKTMQE APKYDDVFAE VNRYFIEQIA RCEQAGIAKE 

       190        200        210        220        230        240 
KLLLDPGFGF GKNLSHNYSL LARLAEFHHF NLPLLVGMSR KSMIGQLLNV GPSERLSGSL 

       250        260        270        280 
ACAVIAAMQG AHIIRVHDVK ETVEAMRVVE ATLSAKENKR YE 

« Hide

References

« Hide 'large scale' references
[1]"Point mutations in the dihydropteroate synthase gene causing sulfonamide resistance."
Swedberg G., Fermer C., Skoeld O.
Adv. Exp. Med. Biol. 338:555-558(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C-167.
[2]"Cloning, sequencing, and enhanced expression of the dihydropteroate synthase gene of Escherichia coli MC4100."
Dallas W.S., Gowen J.E., Ray P.H., Cox M.J., Dev I.K.
J. Bacteriol. 174:5961-5970(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]Wang R., Kushner S.R.
Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100."
Talarico T.L., Dev I.K., Dallas W.S., Ferone R., Ray P.H.
J. Bacteriol. 173:7029-7032(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-28.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[7]"Characterization of mutationally altered dihydropteroate synthase and its ability to form a sulfonamide-containing dihydrofolate analog."
Swedberg G., Castensson S., Skold O.
J. Bacteriol. 137:129-136(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR, CATALYTIC ACTIVITY, FUNCTION.
Strain: C-167.
[8]"Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase."
Achari A., Somers D.O., Champness J.N., Bryant P.K., Rosemond J., Stammers D.K.
Nat. Struct. Biol. 4:490-497(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEXES WITH MANGANESE IONS; SULFANILAMIDE AND 7,8-DIHYDROPTERIN PYROPHOSPHATE ANALOGS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68776 Genomic DNA. Translation: CAA48676.1.
X68777 Genomic DNA. Translation: CAA48677.1.
L06494 Genomic DNA. Translation: AAA23804.1.
L12968 Unassigned DNA. Translation: AAA16123.1.
U01376 Genomic DNA. Translation: AAA97509.1.
U18997 Genomic DNA. Translation: AAA57978.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76209.2.
AP009048 Genomic DNA. Translation: BAE77221.1.
PIRA43326.
RefSeqNP_417644.4. NC_000913.3.
YP_491362.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJ0X-ray2.00A1-282[»]
1AJ2X-ray2.00A1-282[»]
1AJZX-ray2.00A1-282[»]
ProteinModelPortalP0AC13.
SMRP0AC13. Positions 1-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47922N.
IntActP0AC13. 1 interaction.
MINTMINT-1268009.
STRING511145.b3177.

Chemistry

ChEMBLCHEMBL4032.
DrugBankDB01298. Sulfacytine.
DB00576. Sulfamethizole.
DB00263. Sulfisoxazole.

Proteomic databases

PaxDbP0AC13.
PRIDEP0AC13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76209; AAC76209; b3177.
BAE77221; BAE77221; BAE77221.
GeneID12932492.
947691.
KEGGecj:Y75_p3097.
eco:b3177.
PATRIC32121772. VBIEscCol129921_3270.

Organism-specific databases

EchoBASEEB4304.
EcoGeneEG50011. folP.

Phylogenomic databases

eggNOGCOG0294.
HOGENOMHOG000217510.
KOK00796.
OMASIDTYHA.
OrthoDBEOG67T5P5.
PhylomeDBP0AC13.
ProtClustDBPRK11613.

Enzyme and pathway databases

BioCycEcoCyc:H2PTEROATESYNTH-MONOMER.
ECOL316407:JW3144-MONOMER.
MetaCyc:H2PTEROATESYNTH-MONOMER.
SABIO-RKP0AC13.
UniPathwayUPA00077; UER00156.

Gene expression databases

GenevestigatorP0AC13.

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

EvolutionaryTraceP0AC13.
PROP0AC13.

Entry information

Entry nameDHPS_ECOLI
AccessionPrimary (citable) accession number: P0AC13
Secondary accession number(s): P26282, P78110, Q2M935
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: April 16, 2014
This is version 78 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene