Dihydropteroate synthase
Details
- Name
- Dihydropteroate synthase
- Synonyms
- 2.5.1.15
- dhpS
- Dihydropteroate pyrophosphorylase
- Gene Name
- folP
- Organism
- Escherichia coli (strain K12)
- 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
- Metal ion binding
- Specific 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.
- Pfam Domain Function
- Pterin_bind (PF00809)
- 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 - 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]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB00576 Sulfamethizole approved, investigational, vet_approved yes inhibitor Details DB01298 Sulfacytine approved yes inhibitor Details DB00263 Sulfisoxazole approved, vet_approved yes inhibitor Details DB00634 Sulfacetamide approved yes inhibitor Details DB00259 Sulfanilamide approved yes inhibitor Details DB01015 Sulfamethoxazole approved yes antagonist Details DB01581 Sulfamerazine approved, vet_approved yes inhibitor Details DB01582 Sulfamethazine approved, investigational, vet_approved yes inhibitor Details DB06729 Sulfaphenazole approved yes inhibitor Details DB06821 Sulfameter approved yes inhibitor Details DB14033 Acetyl sulfisoxazole approved, vet_approved yes inhibitor Details