Dihydropteroate synthase - Escherichia coli (strain K12)

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P0AC13 (DHPS_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	282 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Antibiotic resistance Folate biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	folic acid biosynthetic process Inferred from mutant phenotype Ref.2. Source: EcoCyc response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW response to drug Inferred from mutant phenotype PubMed 9449266. Source: EcoliWiki tetrahydrofolate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from direct assay Ref.6. Source: EcoCyc
Molecular_function	dihydropteroate synthase activity Inferred from direct assay Ref.6. Source: EcoCyc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 282

282

Dihydropteroate synthase

PRO_0000168207

Regions

Domain

15 – 267

253

Pterin-binding

Region

62 – 63

Substrate binding

Sites

Metal binding

Magnesium

Binding site

Substrate

Binding site

Substrate

Binding site

115

Substrate

Binding site

185

Substrate

Binding site

221

Substrate

Binding site

255

Substrate

Binding site

257

Substrate

Natural variations

Natural variant

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

Experimental info

Sequence conflict

Q → E AA sequence Ref.6

Sequence conflict

R → A in AAA97509. Ref.3

Secondary structure

282

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AC13 [UniParc].

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

282

30,615

        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' referencesShow '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 277:1453-1474(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.

PIR

A43326.

RefSeq

NP_417644.4. NC_000913.2.
YP_491362.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0AC13.

SMR

P0AC13. Positions 1-282.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47922N.

IntAct

P0AC13. 1 interaction.

MINT

MINT-1268009.

STRING

511145.b3177.

Proteomic databases

PaxDb

P0AC13.

PRIDE

P0AC13.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76209; AAC76209; b3177.
BAE77221; BAE77221; BAE77221.

GeneID

12932492.
947691.

KEGG

ecj:Y75_p3097.
eco:b3177.

PATRIC

32121772. VBIEscCol129921_3270.

Organism-specific databases

EchoBASE

EB4304.

EcoGene

EG50011. folP.

Phylogenomic databases

eggNOG

COG0294.

HOGENOM

HOG000217510.

K00796.

OMA

KSMIGNL.

ProtClustDB

PRK11613.

Enzyme and pathway databases

BioCyc

EcoCyc:H2PTEROATESYNTH-MONOMER.
ECOL316407:JW3144-MONOMER.
MetaCyc:H2PTEROATESYNTH-MONOMER.

SABIO-RK

P0AC13.

UniPathway

UPA00077; UER00156.

Gene expression databases

Genevestigator

P0AC13.

Family and domain databases

Gene3D

3.20.20.20. 1 hit.

InterPro

IPR006390. DHP_synth.
IPR011005. Dihydropteroate_synth-like.
IPR000489. Pterin-binding.
[Graphical view]

Pfam

PF00809. Pterin_bind. 1 hit.
[Graphical view]

SUPFAM

SSF51717. DHP_synth_like. 1 hit.

TIGRFAMs

TIGR01496. DHPS. 1 hit.

PROSITE

PS00792. DHPS_1. 1 hit.
PS00793. DHPS_2. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL4032.

DrugBank

DB01298. Sulfacytine.
DB00576. Sulfamethizole.
DB00263. Sulfisoxazole.

EvolutionaryTrace

P0AC13.

Entry information

Entry name

DHPS_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents