Dihydropteroate synthase (P0AC13)

Identification
Name:Dihydropteroate synthase
Synonyms:
  • DHPS
  • Dihydropteroate pyrophosphorylase
Gene Name:folP
Enzyme Class:
Biological Properties
General Function:Involved in dihydropteroate synthase activity
Specific Function:DHPS catalyzes the formation of the immediate precursor of folic acid. It is implicated in resistance to sulfonamide
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.06-Hydroxymethyl dihydropterin + 1.0p-Aminobenzoic acid ↔ 1.07,8-Dihydropteroic acid + 1.0Water
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Pyrophosphate+1.0Thumb
1.06-Hydroxymethyl-dihydropterin pyrophosphate + 1.0p-Aminobenzoic acid → 1.0Pyrophosphate + 1.07,8-Dihydropteroic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0p-Aminobenzoic acid + 1.06-Hydroxymethyl-dihydropterin pyrophosphate → 1.07,8-Dihydropteroic acid + 1.0Pyrophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB211816-Hydroxymethyl dihydropterinMetaboCard
ECMDB211826-Hydroxymethyl-dihydropterin pyrophosphateMetaboCard
ECMDB014127,8-Dihydropteroic acidMetaboCard
ECMDB01392p-Aminobenzoic acidMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
dihydropteroate synthase activity
transferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
cellular aromatic compound metabolic process
cellular metabolic process
folic acid and derivative biosynthetic process
folic acid and derivative metabolic process
metabolic process
pteridine and derivative metabolic process
Gene Properties
Blattner:b3177
Gene OrientationCounterclockwise
Centisome Percentage:71.60
Left Sequence End3322085
Right Sequence End3322933
Gene Sequence:
>849 bp
ATGAGAAACAAACTCTCTTTCGACTTGCAGTTGAGCGCCAGAAAAGCGGCAATCGCTGAA
CGGATTGCCGCCCATAAAATTGCCCGCAGTAAAGTGTCGGTCTTTTTAATGGCGATGTCC
GCTGGCGTGTTTATGGCGATCGGATTTACTTTTTACCTTTCCGTTATCGCCGATGCCCCG
TCTTCACAGGCATTAACCCATCTGGTGGGCGGCCTTTGCTTTACACTCGGCTTTATTTTG
CTGGCGGTTTGCGGCACCAGCCTGTTCACCTCGTCGGTAATGACGGTGATGGCAAAAAGT
CGGGGCGTTATTAGTTGGCGAACTTGGCTGATTAACGCACTTCTGGTGGCCTGCGGTAAT
CTGGCAGGTATTGCCTGTTTCAGTTTGTTAATCTGGTTTTCCGGGCTGGTGATGAGTGAA
AACGCGATGTGGGGAGTCGCGGTTTTACACTGCGCCGAGGGCAAAATGCATCATACATTT
ACTGAATCTGTCAGCCTCGGCATTATGTGCAATCTGATGGTTTGCCTGGCGCTGTGGATG
AGTTATTGCGGGCGTTCGTTATGCGACAAAATCGTCGCCATGATTTTGCCCATCACCCTG
TTTGTCGCCAGTGGCTTTGAGCACTGTATCGCCAATTTGTTTGTGATTCCGTTCGCCATT
GCCATTCGCCATTTCGCCCCTCCCCCCTTCTGGCAGCTGGCGCACAGTAGCGCAGACAAT
TTTCCGGCACTGACGGTCAGCCATTTTATTACCGCCAATCTGCTCCCGGTGATGCTGGGT
AATATTATCGGCGGTGCGGTGCTGGTGAGTATGTGTTATCGGGCTATTTATTTACGTCAG
GAACCCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:282
Protein Molecular Weight:30615
Protein Theoretical pI:6
PDB File:1AJZ
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Dihydropteroate synthase
MKLFAQGTSLDLSHPHVMGILNVTPDSFSDGGTHNSLIDAVKHANLMINAGATIIDVGGE
STRPGAAEVSVEEELQRVIPVVEAIAQRFEVWISVDTSKPEVIRESAKVGAHIINDIRSL
SEPGALEAAAETGLPVCLMHMQGNPKTMQEAPKYDDVFAEVNRYFIEQIARCEQAGIAKE
KLLLDPGFGFGKNLSHNYSLLARLAEFHHFNLPLLVGMSRKSMIGQLLNVGPSERLSGSL
ACAVIAAMQGAHIIRVHDVKETVEAMRVVEATLSAKENKRYE
References
External Links:
ResourceLink
Uniprot ID:P0AC13
Uniprot Name:DHPS_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1805553
PDB ID:1AJZ
Ecogene ID:EG50011
Ecocyc:EG50011
ColiBase:b3177
Kegg Gene:b3177
EchoBASE ID:EB4304
CCDB:DHPS_ECOLI
BacMap:90111553
General Reference:
  • Achari, A., Somers, D. O., Champness, J. N., Bryant, P. K., Rosemond, J., Stammers, D. K. (1997). "Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase." Nat Struct Biol 4:490-497. Pubmed: 9187658
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Dallas, W. S., Gowen, J. E., Ray, P. H., Cox, M. J., Dev, I. K. (1992). "Cloning, sequencing, and enhanced expression of the dihydropteroate synthase gene of Escherichia coli MC4100." J Bacteriol 174:5961-5970. Pubmed: 1522070
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Swedberg, G., Fermer, C., Skold, O. (1993). "Point mutations in the dihydropteroate synthase gene causing sulfonamide resistance." Adv Exp Med Biol 338:555-558. Pubmed: 8304179
  • Talarico, T. L., Dev, I. K., Dallas, W. S., Ferone, R., Ray, P. H. (1991). "Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100." J Bacteriol 173:7029-7032. Pubmed: 1657875