3-dehydroquinate dehydratase

Details

Name
3-dehydroquinate dehydratase
Kind
protein
Synonyms
  • 3-dehydroquinase
  • 4.2.1.10
  • DHQ1
  • Type I dehydroquinase
  • Type I DHQase
Gene Name
aroD
UniProtKB Entry
P24670Swiss-Prot
Organism
Salmonella typhi
NCBI Taxonomy ID
90370
Amino acid sequence
>lcl|BSEQ0011301|3-dehydroquinate dehydratase
MKTVTVKNLIIGEGMPKIIVSLMGRDINSVKAEALAYREATFDILEWRVDHFMDIASTQS
VLTAARVIRDAMPDIPLLFTFRSAKEGGEQTITTQHYLTLNRAAIDSGLVDMIDLELFTG
DADVKATVDYAHAHNVYVVMSNHDFHQTPSAEEMVLRLRKMQALGADIPKIAVMPQSKHD
VLTLLTATLEMQQHYADRPVITMSMAKEGVISRLAGEVFGSAATFGAVKQASAPGQIAVN
DLRSVLMILHNA
Number of residues
252
Molecular Weight
27648.745
Theoretical pI
6.23
GO Classification
Functions
3-dehydroquinate dehydratase activity
Processes
3,4-dihydroxybenzoate biosynthetic process / aromatic amino acid family biosynthetic process / chorismate biosynthetic process
General Function
Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. The reaction involves the formation of an imine intermediate between the keto group of 3-dehydroquinate and the epsilon-amino group of Lys-170 at the active site.
Specific Function
3-dehydroquinate dehydratase activity
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011302|3-dehydroquinate dehydratase (aroD)
ATGAAAACCGTCACCGTAAAAAATCTTATCATTGGCGAAGGGATGCCCAAAATTATCGTG
TCGTTGATGGGAAGAGACATCAATAGCGTGAAAGCGGAGGCGCTGGCCTACCGCGAAGCT
ACATTCGATATTCTGGAGTGGCGCGTGGATCACTTTATGGATATCGCATCGACTCAATCC
GTTCTTACCGCTGCGCGTGTTATCCGCGATGCGATGCCTGACATTCCGTTACTGTTTACT
TTCCGCAGCGCCAAAGAAGGCGGCGAGCAGACAATAACCACTCAGCATTATCTCACGCTT
AATCGTGCCGCAATCGACAGCGGCCTGGTCGATATGATCGATCTTGAGCTATTTACCGGT
GATGCTGACGTTAAAGCCACTGTCGATTATGCCCATGCGCATAATGTTTATGTCGTGATG
TCTAACCACGATTTTCACCAGACGCCGTCCGCAGAGGAAATGGTTCTGCGGCTACGTAAA
ATGCAAGCACTCGGCGCGGATATTCCCAAGATTGCCGTTATGCCGCAAAGCAAGCATGAT
GTATTAACGTTACTCACTGCCACGCTGGAGATGCAGCAACATTACGCCGACCGTCCGGTA
ATTACTATGTCAATGGCGAAAGAGGGTGTCATTTCACGTCTGGCAGGGGAAGTGTTTGGC
TCTGCCGCCACGTTTGGCGCGGTGAAGCAGGCTTCAGCGCCGGGGCAAATCGCCGTAAAT
GATCTACGCAGTGTATTAATGATTCTGCACAACGCCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP24670
UniProtKB Entry NameAROD_SALTI
GenBank Protein ID47642
GenBank Gene IDX54546
PDB ID(s)1GQN, 1L9W, 1QFE, 4CLM, 4CNN, 4CNO, 4CNP, 4UIO
KEGG IDstt:t1231
NCBI Gene ID1248131
General References
  1. Servos S, Chatfield S, Hone D, Levine M, Dimitriadis G, Pickard D, Dougan G, Fairweather N, Charles I: Molecular cloning and characterization of the aroD gene encoding 3-dehydroquinase from Salmonella typhi. J Gen Microbiol. 1991 Jan;137(1):147-52. [Article]
  2. Parkhill J, Dougan G, James KD, Thomson NR, Pickard D, Wain J, Churcher C, Mungall KL, Bentley SD, Holden MT, Sebaihia M, Baker S, Basham D, Brooks K, Chillingworth T, Connerton P, Cronin A, Davis P, Davies RM, Dowd L, White N, Farrar J, Feltwell T, Hamlin N, Haque A, Hien TT, Holroyd S, Jagels K, Krogh A, Larsen TS, Leather S, Moule S, O'Gaora P, Parry C, Quail M, Rutherford K, Simmonds M, Skelton J, Stevens K, Whitehead S, Barrell BG: Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18. Nature. 2001 Oct 25;413(6858):848-52. [Article]
  3. Deng W, Liou SR, Plunkett G 3rd, Mayhew GF, Rose DJ, Burland V, Kodoyianni V, Schwartz DC, Blattner FR: Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18. J Bacteriol. 2003 Apr;185(7):2330-7. [Article]
  4. Gourley DG, Shrive AK, Polikarpov I, Krell T, Coggins JR, Hawkins AR, Isaacs NW, Sawyer L: The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction. Nat Struct Biol. 1999 Jun;6(6):521-5. [Article]
  5. Lee WH, Perles LA, Nagem RA, Shrive AK, Hawkins A, Sawyer L, Polikarpov I: Comparison of different crystal forms of 3-dehydroquinase from Salmonella typhi and its implication for the enzyme activity. Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):798-804. Epub 2002 Apr 26. [Article]
  6. Maneiro M, Peon A, Lence E, Otero JM, Van Raaij MJ, Thompson P, Hawkins AR, Gonzalez-Bello C: Insights into substrate binding and catalysis in bacterial type I dehydroquinase. Biochem J. 2014 Sep 15;462(3):415-24. doi: 10.1042/BJ20140614. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
3-Amino-4,5-Dihydroxy-Cyclohex-1-EnecarboxylateexperimentalunknowntargetDetails