3-dehydroquinate dehydratase
Details
- Name
- 3-dehydroquinate dehydratase
- Synonyms
- 3-dehydroquinase
- 4.2.1.10
- DHQ1
- Type I dehydroquinase
- Type I DHQase
- Gene Name
- aroD
- Organism
- Salmonella typhi
- 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
- Functions3-dehydroquinate dehydratase activityProcesses3,4-dihydroxybenzoate biosynthetic process / aromatic amino acid family biosynthetic process / chorismate biosynthetic process
- General Function
- 3-dehydroquinate dehydratase activity
- Specific 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 epsylon-amino group of Lys-170 at the active site.
- Pfam Domain Function
- DHquinase_I (PF01487)
- 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
Resource Link UniProtKB ID P24670 UniProtKB Entry Name AROD_SALTI GenBank Protein ID 47642 GenBank Gene ID X54546 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]