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0  structures 593  species 0  interactions 821  sequences 12  architectures

Family: DHQS (PF01959)

Summary: 3-dehydroquinate synthase II

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This is the Wikipedia entry entitled "3-dehydroquinate synthase II". More...

3-dehydroquinate synthase II Edit Wikipedia article

3-dehydroquinate synthase II
EC number1.4.1.24
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum

3-dehydroquinate synthase II (EC, DHQ synthase II, MJ1249 (gene), aroB' (gene)) is an enzyme with systematic name 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate:NAD+ oxidoreductase (deaminating).[1] This enzyme catalyses the following chemical reaction

2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + H2O + NAD+ 3-dehydroquinate + NH3 + NADH + H+

The enzyme was isolated from the archaeon Methanocaldococcus jannaschii.


  1. ^ White RH (June 2004). "L-Aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii". Biochemistry. 43 (23): 7618–27. doi:10.1021/bi0495127. PMID 15182204.

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This family includes members of 3-dehydroquinate synthase II ( EC:, encoded by aroB genes in M. maripaludis which is widely distributed in methanogens. In M. jannaschii, proteins ADTH synthase (AroA) and DHQ synthase II (AroB) are required to convert 6-deoxy-5-ketofructose-1-phosphate (DKFP) and aspartate semialdehyde to 3-dehydroquinate (DHQ) in vitro [1, 2].

Literature references

  1. Porat I, Sieprawska-Lupa M, Teng Q, Bohanon FJ, White RH, Whitman WB;, Mol Microbiol. 2006;62:1117-1131.: Biochemical and genetic characterization of an early step in a novel pathway for the biosynthesis of aromatic amino acids and p-aminobenzoic acid in the archaeon Methanococcus maripaludis. PUBMED:17010158 EPMC:17010158

  2. White RH;, Biochemistry. 2004;43:7618-7627.: L-Aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii. PUBMED:15182204 EPMC:15182204

This tab holds annotation information from the InterPro database.

InterPro entry IPR002812

3-Dehydroquinate synthase ( EC ) is an enzyme in the common pathway of aromatic amino acid biosynthesis that catalyses the conversion of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate (DAHP) into 3-dehydroquinic acid [ PUBMED:11173489 ]. This synthesis of aromatic amino acids is an essential metabolic function for most prokaryotic as well as lower eukaryotic cells, including plants. The pathway is absent in humans; therefore, DHQS represents a potential target for the development of novel and selective antimicrobial agents. Owing to the threat posed by the spread of pathogenic bacteria resistant to many currently used antimicrobial drugs, there is clearly a need to develop new anti-infective drugs acting at novel targets. A further potential use for DHQS inhibitors is as herbicides [ PUBMED:11412967 ].

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Seed source: Enright A
Previous IDs: DUF109;
Type: Family
Sequence Ontology: SO:0100021
Author: Enright A , Ouzounis C , Bateman A , El-Gebali S
Number in seed: 78
Number in full: 821
Average length of the domain: 314.20 aa
Average identity of full alignment: 36 %
Average coverage of the sequence by the domain: 90.02 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.2 22.2
Trusted cut-off 22.8 22.4
Noise cut-off 21.7 21.5
Model length: 347
Family (HMM) version: 18
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Family Structural Model

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Improved protein structure prediction using predicted inter-residue orientations. Jianyi Yang, Ivan Anishchenko, Hahnbeom Park, Zhenling Peng, Sergey Ovchinnikov, David Baker Proceedings of the National Academy of Sciences Jan 2020, 117 (3) 1496-1503; DOI: 10.1073/pnas.1914677117;