Dihydropteroate synthase
Details
- Name
- Dihydropteroate synthase
- Synonyms
- 2.5.1.15
- dhpS
- Dihydropteroate pyrophosphorylase
- Gene Name
- folP
- UniProtKB Entry
- P0AC13Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- Amino acid sequence
>lcl|BSEQ0001602|Dihydropteroate synthase MKLFAQGTSLDLSHPHVMGILNVTPDSFSDGGTHNSLIDAVKHANLMINAGATIIDVGGE STRPGAAEVSVEEELQRVIPVVEAIAQRFEVWISVDTSKPEVIRESAKVGAHIINDIRSL SEPGALEAAAETGLPVCLMHMQGNPKTMQEAPKYDDVFAEVNRYFIEQIARCEQAGIAKE KLLLDPGFGFGKNLSHNYSLLARLAEFHHFNLPLLVGMSRKSMIGQLLNVGPSERLSGSL ACAVIAAMQGAHIIRVHDVKETVEAMRVVEATLSAKENKRYE
- Number of residues
- 282
- Molecular Weight
- 30614.855
- Theoretical pI
- 5.95
- GO Classification
- Functionsdihydropteroate synthase activity / metal ion bindingProcessesfolic acid biosynthetic process / response to drug / tetrahydrofolate biosynthetic processComponentscytoplasm / cytosol
- General Function
- Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
- Specific Function
- dihydropteroate synthase activity
- Pfam Domain Function
- Pterin_bind (PF00809)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0010567|Dihydropteroate synthase (folP) ATGAAACTCTTTGCCCAGGGTACTTCACTGGACCTTAGCCATCCTCACGTAATGGGGATC CTCAACGTCACGCCTGATTCCTTTTCGGATGGTGGCACGCATAACTCGCTGATAGATGCG GTGAAACATGCGAATCTGATGATCAACGCTGGCGCGACGATCATTGACGTTGGTGGCGAG TCCACGCGCCCAGGGGCGGCGGAAGTTAGCGTTGAAGAAGAGTTGCAACGTGTTATTCCT GTGGTTGAGGCAATTGCTCAACGCTTCGAAGTCTGGATCTCAGTCGATACATCCAAACCA GAAGTCATCCGTGAGTCAGCGAAAGTTGGCGCTCACATTATTAATGATATCCGCTCCCTT TCCGAACCTGGCGCTCTGGAGGCGGCTGCAGAAACCGGTTTACCGGTTTGTCTGATGCAT ATGCAGGGAAATCCAAAAACCATGCAGGAAGCTCCGAAGTATGACGATGTCTTTGCAGAA GTGAATCGCTACTTTATTGAGCAAATAGCACGTTGCGAGCAGGCGGGTATCGCAAAAGAG AAATTGTTGCTCGACCCCGGATTCGGTTTCGGTAAAAATCTCTCCCATAACTATTCATTA CTGGCGCGCCTGGCTGAATTTCACCATTTCAACCTGCCGCTGTTGGTGGGTATGTCACGA AAATCGATGATTGGGCAGCTGCTGAACGTGGGGCCGTCCGAGCGCCTGAGCGGTAGTCTG GCCTGTGCGGTCATTGCCGCAATGCAAGGCGCGCACATCATTCGTGTTCATGACGTCAAA GAAACCGTAGAAGCGATGCGGGTGGTGGAAGCCACTCTGTCTGCAAAGGAAAACAAACGC TATGAGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0AC13 UniProtKB Entry Name DHPS_ECOLI GenBank Protein ID 41273 GenBank Gene ID X68776 PDB ID(s) 1AJ0, 1AJ2, 1AJZ KEGG ID ecj:JW3144 NCBI Gene ID 947691 - General References
- Swedberg G, Fermer C, Skold O: Point mutations in the dihydropteroate synthase gene causing sulfonamide resistance. Adv Exp Med Biol. 1993;338:555-8. [Article]
- Dallas WS, Gowen JE, Ray PH, Cox MJ, Dev IK: Cloning, sequencing, and enhanced expression of the dihydropteroate synthase gene of Escherichia coli MC4100. J Bacteriol. 1992 Sep;174(18):5961-70. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Talarico TL, Dev IK, Dallas WS, Ferone R, Ray PH: Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100. J Bacteriol. 1991 Nov;173(21):7029-32. [Article]
- Richey DP, Brown GM: The biosynthesis of folic acid. IX. Purification and properties of the enzymes required for the formation of dihydropteroic acid. J Biol Chem. 1969 Mar 25;244(6):1582-92. [Article]
- Swedberg G, Castensson S, Skold O: Characterization of mutationally altered dihydropteroate synthase and its ability to form a sulfonamide-containing dihydrofolate analog. J Bacteriol. 1979 Jan;137(1):129-36. [Article]
- Achari A, Somers DO, Champness JN, Bryant PK, Rosemond J, Stammers DK: Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase. Nat Struct Biol. 1997 Jun;4(6):490-7. [Article]
Associated Data
- Bio-Entities
Bio-Entity Type Dihydropteroate synthase (Escherichia coli (strain K12)) protein primary- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Sulfamethizole approved, investigational, vet_approved yes target inhibitor Details Sulfacytine approved yes target inhibitor Details Sulfisoxazole approved, vet_approved yes target inhibitor Details Sulfacetamide approved yes target inhibitor Details Sulfanilamide approved yes target inhibitor Details Sulfamethoxazole approved yes target antagonist Details Sulfamerazine approved, vet_approved yes target inhibitor Details Sulfamethazine approved, investigational, vet_approved yes target inhibitor Details Sulfaphenazole approved yes target inhibitor Details Sulfameter approved yes target inhibitor Details Acetyl sulfisoxazole approved, vet_approved yes target inhibitor Details 6-hydroxymethylpterin diphosphate experimental yes target inhibitor Details Pterin-6-Yl-Methyl-Monophosphate experimental yes target inhibitor Details 6-Methylamino-5-Nitroisocytosine experimental yes target inhibitor Details Pteroic acid experimental yes target inhibitor Details Ethylenediamine approved, experimental yes target inhibitor Details Sulfametopyrazine approved, withdrawn yes target inhibitor Details Cefozopran experimental yes target inhibitor Details Faropenem investigational yes target inhibitor Details Oritavancin approved, investigational yes target inhibitor Details Sulfadoxine approved, investigational yes target binder Details Sulfapyridine approved yes target inhibitor Details Sulfadiazine approved, investigational, vet_approved yes target inhibitor Details Doripenem approved, investigational yes target inhibitor Details Silver sulfadiazine approved, vet_approved yes target binder Details Polymyxin B approved, vet_approved yes target binder Details Colistin approved yes target binder Details Gramicidin D approved yes target binder Details Daptomycin approved, investigational yes target binder Details Colistimethate approved, vet_approved yes target binder Details