3-dehydroquinate dehydratase
Details
- Name
- 3-dehydroquinate dehydratase
- Synonyms
- 3-dehydroquinase
- 4.2.1.10
- Type II DHQase
- Gene Name
- aroQ
- Organism
- Helicobacter pylori (strain ATCC 700392 / 26695)
- Amino acid sequence
>lcl|BSEQ0019172|3-dehydroquinate dehydratase MKILVIQGPNLNMLGHRDPRLYGMVTLDQIHEIMQTFVKQGNLDVELEFFQTNFEGEIID KIQESVGSDYEGIIINPGAFSHTSIAIADAIMLAGKPVIEVHLTNIQAREEFRKNSYTGA ACGGVIMGFGPLGYNMALMAMVNILAEMKAFQEAQKNNPNNPINNQK
- Number of residues
- 167
- Molecular Weight
- 18483.21
- Theoretical pI
- 4.93
- GO Classification
- Functions3-dehydroquinate dehydratase activityProcessesaromatic amino acid family biosynthetic process / chorismate biosynthetic process
- General Function
- 3-dehydroquinate dehydratase activity
- Specific Function
- Catalyzes a trans-dehydration via an enolate intermediate.
- Pfam Domain Function
- DHquinase_II (PF01220)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0019173|3-dehydroquinate dehydratase (aroQ) ATGAAAATTTTAGTGATTCAAGGGCCTAATTTAAACATGTTAGGACACAGAGACCCAAGG CTTTATGGTATGGTAACCTTAGACCAAATCCATGAAATCATGCAAACTTTCGTGAAACAA GGCAATTTAGATGTGGAATTAGAGTTTTTTCAAACTAATTTTGAGGGCGAAATCATTGAT AAAATCCAAGAGAGCGTGGGCAGCGATTATGAAGGGATCATCATTAACCCTGGAGCGTTT TCGCACACTTCTATTGCGATTGCAGATGCGATCATGCTAGCGGGCAAACCCGTTATTGAA GTGCATCTCACTAACATTCAAGCCAGAGAGGAATTCAGGAAAAATTCTTACACTGGAGCG GCTTGTGGAGGCGTGATCATGGGATTTGGCCCGCTTGGCTACAACATGGCTTTAATGGCG ATGGTCAATATTTTAGCCGAAATGAAAGCGTTCCAAGAAGCCCAAAAAAACAACCCTAAT AACCCCATTAACAATCAAAAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q48255 UniProtKB Entry Name AROQ_HELPY GenBank Protein ID 2314182 GenBank Gene ID AE000511 - General References
- Bottomley JR, Clayton CL, Chalk PA, Kleanthous C: Cloning, sequencing, expression, purification and preliminary characterization of a type II dehydroquinase from Helicobacter pylori. Biochem J. 1996 Oct 15;319 ( Pt 2):559-65. [Article]
- Tomb JF, White O, Kerlavage AR, Clayton RA, Sutton GG, Fleischmann RD, Ketchum KA, Klenk HP, Gill S, Dougherty BA, Nelson K, Quackenbush J, Zhou L, Kirkness EF, Peterson S, Loftus B, Richardson D, Dodson R, Khalak HG, Glodek A, McKenney K, Fitzegerald LM, Lee N, Adams MD, Hickey EK, Berg DE, Gocayne JD, Utterback TR, Peterson JD, Kelley JM, Cotton MD, Weidman JM, Fujii C, Bowman C, Watthey L, Wallin E, Hayes WS, Borodovsky M, Karp PD, Smith HO, Fraser CM, Venter JC: The complete genome sequence of the gastric pathogen Helicobacter pylori. Nature. 1997 Aug 7;388(6642):539-47. [Article]
- Lee BI, Kwak JE, Suh SW: Crystal structure of the type II 3-dehydroquinase from Helicobacter pylori. Proteins. 2003 Jun 1;51(4):616-7. [Article]
- Robinson DA, Stewart KA, Price NC, Chalk PA, Coggins JR, Lapthorn AJ: Crystal structures of Helicobacter pylori type II dehydroquinase inhibitor complexes: new directions for inhibitor design. J Med Chem. 2006 Feb 23;49(4):1282-90. [Article]