Dihydropteroate synthase
Details
- Name
- Dihydropteroate synthase
- Synonyms
- 2.5.1.15
- DHPS
- Dihydropteroate pyrophosphorylase
- Gene Name
- folP
- Organism
- Bacillus anthracis
- Amino acid sequence
>lcl|BSEQ0012191|Dihydropteroate synthase MCSLKWDYDLRCGEYTLNLNEKTLIMGILNVTPDSFSDGGSYNEVDAAVRHAKEMRDEGA HIIDIGGESTRPGFAKVSVEEEIKRVVPMIQAVSKEVKLPISIDTYKAEVAKQAIEAGAH IINDIWGAKAEPKIAEVAAHYDVPIILMHNRDNMNYRNLMADMIADLYDSIKIAKDAGVR DENIILDPGIGFAKTPEQNLEAMRNLEQLNVLGYPVLLGTSRKSFIGHVLDLPVEERLEG TGATVCLGIEKGCEFVRVHDVKEMSRMAKMMDAMIGKGVK
- Number of residues
- 280
- Molecular Weight
- 30975.455
- Theoretical pI
- 5.0
- GO Classification
- Functionsdihydropteroate synthase activity / metal ion bindingProcessesfolic acid biosynthetic process / tetrahydrofolate biosynthetic process
- 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|BSEQ0012192|Dihydropteroate synthase (folP) ATGTGTAGTTTGAAGTGGGATTATGATTTGCGCTGCGGCGAATATACATTGAACTTAAAT GAAAAAACATTAATTATGGGGATTTTAAATGTAACACCAGATTCGTTTTCTGATGGTGGG AGTTATAATGAGGTAGATGCTGCAGTGCGCCATGCGAAAGAAATGCGAGATGAAGGTGCT CATATTATTGATATTGGTGGCGAATCTACTCGTCCGGGTTTTGCTAAAGTATCGGTGGAA GAAGAAATAAAACGAGTTGTTCCGATGATTCAGGCTGTTTCAAAAGAGGTAAAATTGCCT ATTTCTATCGACACGTATAAAGCTGAAGTTGCAAAACAAGCAATTGAAGCTGGTGCTCAT ATTATTAATGATATTTGGGGAGCGAAGGCAGAACCAAAAATCGCTGAAGTTGCAGCTCAT TACGATGTACCTATTATCTTAATGCACAATCGCGATAACATGAATTATCGCAATTTAATG GCTGATATGATTGCTGACTTATATGACAGTATTAAAATTGCTAAAGATGCTGGTGTGCGA GATGAGAATATCATTTTAGACCCGGGTATCGGTTTTGCTAAAACACCTGAACAAAATTTA GAAGCGATGCGTAATTTAGAACAGTTAAACGTACTAGGTTATCCAGTTCTCTTAGGTACT TCAAGAAAGTCCTTTATTGGGCATGTGCTAGATTTACCGGTAGAAGAACGTCTTGAGGGA ACGGGAGCTACCGTTTGTCTTGGTATTGAAAAGGGTTGTGAGTTTGTTCGCGTTCATGAT GTGAAGGAAATGTCGCGTATGGCTAAGATGATGGATGCGATGATTGGTAAGGGGGTAAAG TAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q81VW8 UniProtKB Entry Name Q81VW8_BACAN GenBank Gene ID AE016879 - General References
- Babaoglu K, Qi J, Lee RE, White SW: Crystal structure of 7,8-dihydropteroate synthase from Bacillus anthracis: mechanism and novel inhibitor design. Structure. 2004 Sep;12(9):1705-17. [Article]
- Valderas MW, Bourne PC, Barrow WW: Genetic basis for sulfonamide resistance in Bacillus anthracis. Microb Drug Resist. 2007 Spring;13(1):11-20. [Article]
- Ravel J, Jiang L, Stanley ST, Wilson MR, Decker RS, Read TD, Worsham P, Keim PS, Salzberg SL, Fraser-Liggett CM, Rasko DA: The complete genome sequence of Bacillus anthracis Ames "Ancestor". J Bacteriol. 2009 Jan;191(1):445-6. doi: 10.1128/JB.01347-08. Epub 2008 Oct 24. [Article]
- Hevener KE, Yun MK, Qi J, Kerr ID, Babaoglu K, Hurdle JG, Balakrishna K, White SW, Lee RE: Structural studies of pterin-based inhibitors of dihydropteroate synthase. J Med Chem. 2010 Jan 14;53(1):166-77. doi: 10.1021/jm900861d. [Article]
- Zhao Y, Hammoudeh D, Yun MK, Qi J, White SW, Lee RE: Structure-based design of novel pyrimido[4,5-c]pyridazine derivatives as dihydropteroate synthase inhibitors with increased affinity. ChemMedChem. 2012 May;7(5):861-70. doi: 10.1002/cmdc.201200049. Epub 2012 Mar 13. [Article]
- Yun MK, Wu Y, Li Z, Zhao Y, Waddell MB, Ferreira AM, Lee RE, Bashford D, White SW: Catalysis and sulfa drug resistance in dihydropteroate synthase. Science. 2012 Mar 2;335(6072):1110-4. doi: 10.1126/science.1214641. [Article]
- Hammoudeh DI, Date M, Yun MK, Zhang W, Boyd VA, Viacava Follis A, Griffith E, Lee RE, Bashford D, White SW: Identification and characterization of an allosteric inhibitory site on dihydropteroate synthase. ACS Chem Biol. 2014 Jun 20;9(6):1294-302. doi: 10.1021/cb500038g. Epub 2014 Mar 27. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB03592 Pterin-6-Yl-Methyl-Monophosphate experimental unknown Details DB03705 6-Methylamino-5-Nitroisocytosine experimental unknown Details DB04047 6-hydroxymethylpterin diphosphate experimental unknown Details DB04196 Pteroic acid experimental unknown Details