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P0AC13

- DHPS_ECOLI

UniProt

P0AC13 - DHPS_ECOLI

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Protein

Dihydropteroate synthase

Gene
folP, dhpS, b3177, JW3144
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

Binds 1 magnesium 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: EcoCyc
  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: EcoCyc
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 – 54
Beta strandi8 – 114
Beta strandi16 – 227
Turni25 – 273
Helixi29 – 335
Helixi36 – 5015
Beta strandi53 – 608
Helixi71 – 8818
Beta strandi92 – 965
Helixi100 – 1089
Beta strandi113 – 1164
Turni117 – 1204
Helixi125 – 1328
Beta strandi136 – 1394
Helixi157 – 17418
Helixi179 – 1813
Beta strandi182 – 1854
Helixi194 – 2029
Helixi204 – 2107
Beta strandi214 – 2163
Helixi222 – 2287
Helixi232 – 2343
Helixi236 – 24813
Beta strandi252 – 2576
Helixi259 – 27517

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJ0X-ray2.00A1-282[»]
1AJ2X-ray2.00A1-282[»]
1AJZX-ray2.00A1-282[»]
ProteinModelPortaliP0AC13.
SMRiP0AC13. Positions 1-282.

Miscellaneous databases

EvolutionaryTraceiP0AC13.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 267253Pterin-bindingAdd
BLAST

Region

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

Sequence similaritiesi

Belongs to the DHPS family.

Phylogenomic databases

eggNOGiCOG0294.
HOGENOMiHOG000217510.
KOiK00796.
OMAiDCWISVD.
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

MKLFAQGTSL DLSHPHVMGI LNVTPDSFSD GGTHNSLIDA VKHANLMINA    50
GATIIDVGGE STRPGAAEVS VEEELQRVIP VVEAIAQRFE VWISVDTSKP 100
EVIRESAKVG AHIINDIRSL SEPGALEAAA ETGLPVCLMH MQGNPKTMQE 150
APKYDDVFAE VNRYFIEQIA RCEQAGIAKE KLLLDPGFGF GKNLSHNYSL 200
LARLAEFHHF NLPLLVGMSR KSMIGQLLNV GPSERLSGSL ACAVIAAMQG 250
AHIIRVHDVK ETVEAMRVVE ATLSAKENKR YE 282
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.

Natural variant

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

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi A43326.
RefSeqi NP_417644.4. NC_000913.3.
YP_491362.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AJ0 X-ray 2.00 A 1-282 [» ]
1AJ2 X-ray 2.00 A 1-282 [» ]
1AJZ X-ray 2.00 A 1-282 [» ]
ProteinModelPortali P0AC13.
SMRi P0AC13. Positions 1-282.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-47922N.
IntActi P0AC13. 1 interaction.
MINTi MINT-1268009.
STRINGi 511145.b3177.

Chemistry

ChEMBLi CHEMBL4032.
DrugBanki DB01298. Sulfacytine.
DB00576. Sulfamethizole.
DB00263. Sulfisoxazole.

Proteomic databases

PaxDbi P0AC13.
PRIDEi P0AC13.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76209 ; AAC76209 ; b3177 .
BAE77221 ; BAE77221 ; BAE77221 .
GeneIDi 12932492.
947691.
KEGGi ecj:Y75_p3097.
eco:b3177.
PATRICi 32121772. VBIEscCol129921_3270.

Organism-specific databases

EchoBASEi EB4304.
EcoGenei EG50011. folP.

Phylogenomic databases

eggNOGi COG0294.
HOGENOMi HOG000217510.
KOi K00796.
OMAi DCWISVD.
OrthoDBi EOG67T5P5.
PhylomeDBi P0AC13.

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00156 .
BioCyci EcoCyc:H2PTEROATESYNTH-MONOMER.
ECOL316407:JW3144-MONOMER.
MetaCyc:H2PTEROATESYNTH-MONOMER.
SABIO-RK P0AC13.

Miscellaneous databases

EvolutionaryTracei P0AC13.
PROi P0AC13.

Gene expression databases

Genevestigatori P0AC13.

Family and domain databases

Gene3Di 3.20.20.20. 1 hit.
InterProi IPR006390. DHP_synth.
IPR011005. Dihydropteroate_synth-like.
IPR000489. Pterin-binding.
[Graphical view ]
Pfami PF00809. Pterin_bind. 1 hit.
[Graphical view ]
SUPFAMi SSF51717. SSF51717. 1 hit.
TIGRFAMsi TIGR01496. DHPS. 1 hit.
PROSITEi PS00792. DHPS_1. 1 hit.
PS00793. DHPS_2. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: May 14, 2014
This is version 79 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

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