Dihydropteroate synthase
Details
- Name
- Dihydropteroate synthase
- Synonyms
- 2.5.1.15
- DHPS
- Dihydropteroate pyrophosphorylase
- folP
- Gene Name
- folP1
- UniProtKB Entry
- P0C0X1Swiss-Prot
- Organism
- Mycobacterium leprae (strain TN)
- NCBI Taxonomy ID
- 272631
- Amino acid sequence
>lcl|BSEQ0011512|Dihydropteroate synthase MSLAPVQVIGVLNVTDNSFSDGGRYLDPDDAVQHGLAMVAEGAAIVDVGGESTRPGAIRT DPRVELSRIVPVVKELAAQGITVSIDTTRADVARAALQSGARIVNDVSGGRADPAMAPLV AEAGVAWVLMHWRLMSAERPYEAPNYRDVVAEVRADLLAGVDQAVAAGVDPGSLVIDPGL GFAKTGQHNWALLNALPELVATGVPILLGASRKRFLGRLLAGADGAVRPPDGRETATAVI SALAALHGAWGVRVHDVRASVDALKVVGAWLHAGPQIEKVRCDG
- Number of residues
- 284
- Molecular Weight
- 29447.355
- Theoretical pI
- 5.63
- 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, the immediate precursor of folate derivatives.
- Pfam Domain Function
- Pterin_bind (PF00809)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011513|Dihydropteroate synthase (folP1) GTGAGTTTGGCGCCAGTGCAGGTTATTGGGGTTTTGAACGTCACTGACAATTCGTTCTCA GATGGCGGACGTTACCTTGATCCTGACGATGCTGTCCAGCACGGCCTGGCAATGGTCGCG GAAGGCGCGGCGATTGTCGACGTCGGTGGCGAATCGACCCGGCCCGGTGCCATTAGGACC GATCCTCGAGTTGAACTCTCTCGTATCGTTCCTGTCGTAAAAGAACTTGCAGCACAGGGG ATTACAGTAAGTATCGATACTACGCGCGCTGATGTTGCACGGGCGGCGCTGCAAAGCGGC GCACGGATCGTCAACGATGTGTCTGGTGGGCGAGCAGATCCCGCGATGGCTCCTCTGGTG GCTGAAGCCGGTGTTGCGTGGGTGTTGATGCACTGGCGACTGATGTCGGCTGAACGGCCG TATGAGGCTCCGAATTACCGCGACGTGGTGGCTGAAGTGCGTGCCGACCTACTGGCTGGT GTCGATCAGGCTGTGGCCGCAGGTGTTGATCCTGGGAGTCTAGTGATCGATCCCGGGCTT GGATTCGCCAAGACGGGACAGCACAATTGGGCGCTGCTGAATGCGTTACCGGAGTTGGTG GCTACTGGGGTCCCGATTCTACTTGGCGCCTCGCGTAAACGGTTCCTGGGTAGGTTATTA GCTGGGGCTGATGGCGCGGTACGACCGCCGGACGGACGTGAGACGGCGACCGCGGTGATT TCCGCACTTGCTGCCCTACACGGGGCTTGGGGTGTTCGGGTGCACGATGTGCGTGCCTCG GTCGACGCACTCAAGGTCGTCGGGGCTTGGCTGCATGCTGGGCCGCAGATTGAAAAGGTT AGATGTGATGGCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0C0X1 UniProtKB Entry Name DHPS1_MYCLE GenBank Protein ID 5832717 GenBank Gene ID AB028658 KEGG ID mle:ML0224 NCBI Gene ID 908646 - General References
- Kai M, Matsuoka M, Nakata N, Maeda S, Gidoh M, Maeda Y, Hashimoto K, Kobayashi K, Kashiwabara Y: Diaminodiphenylsulfone resistance of Mycobacterium leprae due to mutations in the dihydropteroate synthase gene. FEMS Microbiol Lett. 1999 Aug 15;177(2):231-5. [Article]
- Nopponpunth V, Sirawaraporn W, Greene PJ, Santi DV: Cloning and expression of Mycobacterium tuberculosis and Mycobacterium leprae dihydropteroate synthase in Escherichia coli. J Bacteriol. 1999 Nov;181(21):6814-21. [Article]
- Cole ST, Eiglmeier K, Parkhill J, James KD, Thomson NR, Wheeler PR, Honore N, Garnier T, Churcher C, Harris D, Mungall K, Basham D, Brown D, Chillingworth T, Connor R, Davies RM, Devlin K, Duthoy S, Feltwell T, Fraser A, Hamlin N, Holroyd S, Hornsby T, Jagels K, Lacroix C, Maclean J, Moule S, Murphy L, Oliver K, Quail MA, Rajandream MA, Rutherford KM, Rutter S, Seeger K, Simon S, Simmonds M, Skelton J, Squares R, Squares S, Stevens K, Taylor K, Whitehead S, Woodward JR, Barrell BG: Massive gene decay in the leprosy bacillus. Nature. 2001 Feb 22;409(6823):1007-11. [Article]
Associated Data
- Bio-Entities
Bio-Entity Type Dihydropteroate synthase (Mycobacterium leprae (strain TN)) protein primary- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Dapsone approved, investigational yes target inhibitor Details