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Protein

Dihydropteroate synthase

Gene

folP

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DHPS catalyzes the formation of the immediate precursor of folic acid. It is implicated in resistance to sulfonamide.1 Publication

Catalytic activityi

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

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit. Magnesium is required for activity, even if it interacts primarily with the substrate.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi22 – 221Magnesium
Binding sitei30 – 301Substrate
Binding sitei96 – 961Substrate
Binding sitei115 – 1151Substrate
Binding sitei185 – 1851Substrate
Binding sitei221 – 2211Substrate
Binding sitei255 – 2551Substrate
Binding sitei257 – 2571Substrate

GO - Molecular functioni

  1. dihydropteroate synthase activity Source: EcoliWiki
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. folic acid biosynthetic process Source: EcoCyc
  2. response to antibiotic Source: UniProtKB-KW
  3. response to drug Source: EcoliWiki
  4. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Antibiotic resistance, Folate biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:H2PTEROATESYNTH-MONOMER.
ECOL316407:JW3144-MONOMER.
MetaCyc:H2PTEROATESYNTH-MONOMER.
SABIO-RKP0AC13.
UniPathwayiUPA00077; UER00156.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydropteroate synthase (EC:2.5.1.15)
Short name:
DHPS
Alternative name(s):
Dihydropteroate pyrophosphorylase
Gene namesi
Name:folP
Synonyms:dhpS
Ordered Locus Names:b3177, JW3144
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG50011. folP.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoliWiki
Complete GO annotation...

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 282282Dihydropteroate synthasePRO_0000168207Add
BLAST

Proteomic databases

PaxDbiP0AC13.
PRIDEiP0AC13.

Expressioni

Gene expression databases

GenevestigatoriP0AC13.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-47922N.
IntActiP0AC13. 1 interaction.
MINTiMINT-1268009.
STRINGi511145.b3177.

Structurei

Secondary structure

1
282
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Beta strandi8 – 114Combined sources
Beta strandi16 – 227Combined sources
Turni25 – 273Combined sources
Helixi29 – 335Combined sources
Helixi36 – 5015Combined sources
Beta strandi53 – 608Combined sources
Helixi71 – 8818Combined sources
Beta strandi92 – 965Combined sources
Helixi100 – 1089Combined sources
Beta strandi113 – 1164Combined sources
Turni117 – 1204Combined sources
Helixi125 – 1328Combined sources
Beta strandi136 – 1394Combined sources
Helixi157 – 17418Combined sources
Helixi179 – 1813Combined sources
Beta strandi182 – 1854Combined sources
Helixi194 – 2029Combined sources
Helixi204 – 2107Combined sources
Beta strandi214 – 2163Combined sources
Helixi222 – 2287Combined sources
Helixi232 – 2343Combined sources
Helixi236 – 24813Combined sources
Beta strandi252 – 2576Combined sources
Helixi259 – 27517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJ0X-ray2.00A1-282[»]
1AJ2X-ray2.00A1-282[»]
1AJZX-ray2.00A1-282[»]
ProteinModelPortaliP0AC13.
SMRiP0AC13. Positions 1-282.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AC13.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 267253Pterin-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni62 – 632Substrate binding

Sequence similaritiesi

Belongs to the DHPS family.Curated
Contains 1 pterin-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0294.
HOGENOMiHOG000217510.
InParanoidiP0AC13.
KOiK00796.
OMAiSIDTYHA.
OrthoDBiEOG67T5P5.
PhylomeDBiP0AC13.

Family and domain databases

Gene3Di3.20.20.20. 1 hit.
InterProiIPR006390. DHP_synth.
IPR011005. Dihydropteroate_synth-like.
IPR000489. Pterin-binding.
[Graphical view]
PfamiPF00809. Pterin_bind. 1 hit.
[Graphical view]
SUPFAMiSSF51717. SSF51717. 1 hit.
TIGRFAMsiTIGR01496. DHPS. 1 hit.
PROSITEiPS00792. DHPS_1. 1 hit.
PS00793. DHPS_2. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AC13-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLFAQGTSL DLSHPHVMGI LNVTPDSFSD GGTHNSLIDA VKHANLMINA
60 70 80 90 100
GATIIDVGGE STRPGAAEVS VEEELQRVIP VVEAIAQRFE VWISVDTSKP
110 120 130 140 150
EVIRESAKVG AHIINDIRSL SEPGALEAAA ETGLPVCLMH MQGNPKTMQE
160 170 180 190 200
APKYDDVFAE VNRYFIEQIA RCEQAGIAKE KLLLDPGFGF GKNLSHNYSL
210 220 230 240 250
LARLAEFHHF NLPLLVGMSR KSMIGQLLNV GPSERLSGSL ACAVIAAMQG
260 270 280
AHIIRVHDVK ETVEAMRVVE ATLSAKENKR YE
Length:282
Mass (Da):30,615
Last modified:November 8, 2005 - v1
Checksum:i6230C8883796F59E
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61Q → E AA sequence (PubMed:1657875)Curated
Sequence conflicti77 – 771R → A in AAA97509. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti28 – 281F → I in TS20; resistant to sulfonamide and temperature-sensitive.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA43326.
RefSeqiNP_417644.4. NC_000913.3.
YP_491362.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76209; AAC76209; b3177.
BAE77221; BAE77221; BAE77221.
GeneIDi12932492.
947691.
KEGGiecj:Y75_p3097.
eco:b3177.
PATRICi32121772. VBIEscCol129921_3270.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA43326.
RefSeqiNP_417644.4. NC_000913.3.
YP_491362.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJ0X-ray2.00A1-282[»]
1AJ2X-ray2.00A1-282[»]
1AJZX-ray2.00A1-282[»]
ProteinModelPortaliP0AC13.
SMRiP0AC13. Positions 1-282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-47922N.
IntActiP0AC13. 1 interaction.
MINTiMINT-1268009.
STRINGi511145.b3177.

Chemistry

BindingDBiP0AC13.
ChEMBLiCHEMBL4032.
DrugBankiDB00634. Sulfacetamide.
DB01298. Sulfacytine.
DB01581. Sulfamerazine.
DB01582. Sulfamethazine.
DB00576. Sulfamethizole.
DB01015. Sulfamethoxazole.
DB00259. Sulfanilamide.
DB06729. Sulfaphenazole.
DB00263. Sulfisoxazole.

Proteomic databases

PaxDbiP0AC13.
PRIDEiP0AC13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76209; AAC76209; b3177.
BAE77221; BAE77221; BAE77221.
GeneIDi12932492.
947691.
KEGGiecj:Y75_p3097.
eco:b3177.
PATRICi32121772. VBIEscCol129921_3270.

Organism-specific databases

EchoBASEiEB4304.
EcoGeneiEG50011. folP.

Phylogenomic databases

eggNOGiCOG0294.
HOGENOMiHOG000217510.
InParanoidiP0AC13.
KOiK00796.
OMAiSIDTYHA.
OrthoDBiEOG67T5P5.
PhylomeDBiP0AC13.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00156.
BioCyciEcoCyc:H2PTEROATESYNTH-MONOMER.
ECOL316407:JW3144-MONOMER.
MetaCyc:H2PTEROATESYNTH-MONOMER.
SABIO-RKP0AC13.

Miscellaneous databases

EvolutionaryTraceiP0AC13.
PROiP0AC13.

Gene expression databases

GenevestigatoriP0AC13.

Family and domain databases

Gene3Di3.20.20.20. 1 hit.
InterProiIPR006390. DHP_synth.
IPR011005. Dihydropteroate_synth-like.
IPR000489. Pterin-binding.
[Graphical view]
PfamiPF00809. Pterin_bind. 1 hit.
[Graphical view]
SUPFAMiSSF51717. SSF51717. 1 hit.
TIGRFAMsiTIGR01496. DHPS. 1 hit.
PROSITEiPS00792. DHPS_1. 1 hit.
PS00793. DHPS_2. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiDHPS_ECOLI
AccessioniPrimary (citable) accession number: P0AC13
Secondary accession number(s): P26282, P78110, Q2M935
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: January 7, 2015
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.