3-dehydroquinate dehydratase
Details
- Name
- 3-dehydroquinate dehydratase
- Synonyms
- 3-dehydroquinase
- 4.2.1.10
- Type II DHQase
- Gene Name
- aroQ
- Organism
- Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
- Amino acid sequence
>lcl|BSEQ0011264|3-dehydroquinate dehydratase MPRSLANAPIMILNGPNLNLLGQRQPEIYGSDTLADVEALCVKAAAAHGGTVDFRQSNHE GELVDWIHEARLNHCGIVINPAAYSHTSVAILDALNTCDGLPVVEVHISNIHQREPFRHH SYVSQRADGVVAGCGVQGYVFGVERIAALAGAGSARA
- Number of residues
- 157
- Molecular Weight
- 16681.69
- Theoretical pI
- 6.41
- 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|BSEQ0011265|3-dehydroquinate dehydratase (aroQ) GTGCCCCGCAGCCTGGCCAACGCCCCGATCATGATCCTCAACGGCCCCAACCTGAACCTG CTCGGCCAGCGCCAGCCGGAGATCTACGGCTCCGACACCCTCGCCGACGTCGAGGCGCTG TGCGTGAAGGCGGCGGCCGCGCACGGCGGCACGGTGGACTTCCGGCAGTCCAACCACGAG GGCGAACTGGTCGACTGGATCCACGAGGCCCGGCTGAACCACTGCGGGATCGTGATCAAC CCCGCCGCCTACTCGCACACGTCCGTCGCCATCCTGGATGCGCTCAACACCTGCGACGGG CTGCCGGTGGTGGAGGTCCACATCTCCAACATCCACCAGCGTGAGCCGTTCCGGCACCAC TCCTACGTCTCGCAGCGCGCCGACGGCGTCGTCGCGGGGTGCGGTGTGCAGGGGTACGTC TTCGGTGTGGAGCGGATCGCCGCCCTGGCCGGGGCGGGCTCGGCCAGGGCCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P15474 UniProtKB Entry Name AROQ_STRCO GenBank Protein ID 2558614 GenBank Gene ID AJ001493 - General References
- Bentley SD, Chater KF, Cerdeno-Tarraga AM, Challis GL, Thomson NR, James KD, Harris DE, Quail MA, Kieser H, Harper D, Bateman A, Brown S, Chandra G, Chen CW, Collins M, Cronin A, Fraser A, Goble A, Hidalgo J, Hornsby T, Howarth S, Huang CH, Kieser T, Larke L, Murphy L, Oliver K, O'Neil S, Rabbinowitsch E, Rajandream MA, Rutherford K, Rutter S, Seeger K, Saunders D, Sharp S, Squares R, Squares S, Taylor K, Warren T, Wietzorrek A, Woodward J, Barrell BG, Parkhill J, Hopwood DA: Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2). Nature. 2002 May 9;417(6885):141-7. [Article]
- White PJ, Young J, Hunter IS, Nimmo HG, Coggins JR: The purification and characterization of 3-dehydroquinase from Streptomyces coelicolor. Biochem J. 1990 Feb 1;265(3):735-8. [Article]
- Krell T, Horsburgh MJ, Cooper A, Kelly SM, Coggins JR: Localization of the active site of type II dehydroquinases. Identification of a common arginine-containing motif in the two classes of dehydroquinases. J Biol Chem. 1996 Oct 4;271(40):24492-7. [Article]
- Roszak AW, Robinson DA, Krell T, Hunter IS, Fredrickson M, Abell C, Coggins JR, Lapthorn AJ: The structure and mechanism of the type II dehydroquinase from Streptomyces coelicolor. Structure. 2002 Apr;10(4):493-503. [Article]
- Frederickson M, Roszak AW, Coggins JR, Lapthorn AJ, Abell C: (1R,4S,5R)-3-Fluoro-1,4,5-trihydroxy-2-cyclohexene-1-carboxylic acid: the fluoro analogue of the enolate intermediate in the reaction catalyzed by type II dehydroquinases. Org Biomol Chem. 2004 Jun 7;2(11):1592-6. Epub 2004 May 6. [Article]
- Toscano MD, Stewart KA, Coggins JR, Lapthorn AJ, Abell C: Rational design of new bifunctional inhibitors of type II dehydroquinase. Org Biomol Chem. 2005 Sep 7;3(17):3102-4. Epub 2005 Aug 1. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB02786 2-Anhydro-3-Fluoro-Quinic Acid experimental unknown Details DB02801 2,3-Anhydro-quinic acid experimental unknown Details DB04347 3-Dehydroshikimate experimental unknown Details DB04656 1,3,4-TRIHYDROXY-5-(3-PHENOXYPROPYL)-CYCLOHEXANE-1-CARBOXYLIC A CID experimental unknown Details DB08485 (1S,4S,5S)-1,4,5-TRIHYDROXY-3-[3-(PHENYLTHIO)PHENYL]CYCLOHEX-2-ENE-1-CARBOXYLIC ACID experimental unknown Details