P05195 · 3DHQ_NEUCR
- ProteinCatabolic 3-dehydroquinase
- Geneqa-2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids173 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
3-dehydroquinate dehydratase; part of the qa gene cluster that mediates the catabolism of quinic acid (QA) and as such, allows the use of QA as a sole carbon source (By similarity) (PubMed:126226, PubMed:143663, PubMed:2525625, PubMed:6458044).
Catalyzes the second reaction in the inducible quinic acid catabolic pathway by converting 3-dehydroquinate into 3-dehydroshikimate (PubMed:143663). The qa cluster encodes 3 inducible enymes (qa-2, qa-3 and qa-4) catalyzing the first three reactions in the catabolism of quinic acid to protocatechuic acid (also known as 3,4-Dihydroxybenzoic acid) (Probable)
Catalyzes the second reaction in the inducible quinic acid catabolic pathway by converting 3-dehydroquinate into 3-dehydroshikimate (PubMed:143663). The qa cluster encodes 3 inducible enymes (qa-2, qa-3 and qa-4) catalyzing the first three reactions in the catabolism of quinic acid to protocatechuic acid (also known as 3,4-Dihydroxybenzoic acid) (Probable)
Catalytic activity
- 3-dehydroquinate = 3-dehydroshikimate + H2OThis reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
450 μM | quinate | |||||
1.7 mM | shikimate | |||||
150 μM | NAD+ |
Pathway
Aromatic compound metabolism; 3,4-dihydroxybenzoate biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 1/2.
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 21 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 26 | Proton acceptor | ||||
Sequence: Y | ||||||
Binding site | 102 | substrate | ||||
Sequence: N | ||||||
Binding site | 108 | substrate | ||||
Sequence: H | ||||||
Binding site | 115 | substrate | ||||
Sequence: D | ||||||
Active site | 128 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 129-130 | substrate | ||||
Sequence: VS | ||||||
Binding site | 139 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 3-dehydroquinate dehydratase activity | |
Biological Process | 3,4-dihydroxybenzoate biosynthetic process | |
Biological Process | quinate catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCatabolic 3-dehydroquinase
- EC number
- Short namescDHQase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Sordariales > Sordariaceae > Neurospora
Accessions
- Primary accessionP05195
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000159948 | 1-173 | Catabolic 3-dehydroquinase | |||
Sequence: MASPRHILLINGPNLNLLGTREPQIYGSTTLHDIEQASQTLASSLGLRLTTFQSNHEGAIIDRIHQAAGFVPSPPSPSPSSAATTTEAGLGPGDKVSAIIINPGAYTHTSIGIRDALLGTGIPFVEVHVSNVHAREAFRHHSYLSDKAVAVICGLGPFGYSAALDFLGRHMKF |
Proteomic databases
Expression
Induction
Expression is induced in the presence of quinic acid (PubMed:144915, PubMed:6458044).
The quinic acid (qa) gene cluster is subject to two levels of gene control: a primary system which responds to the presence of quinic acid via the qa-1S repressor protein that blocks the qa-1F activator, and a secondary system which represses transcription of qa genes in the presence of a preferred carbon source such as glucose (PubMed:12477937, PubMed:17597928, PubMed:19236936, PubMed:6458044).
The quinic acid (qa) gene cluster is subject to two levels of gene control: a primary system which responds to the presence of quinic acid via the qa-1S repressor protein that blocks the qa-1F activator, and a secondary system which represses transcription of qa genes in the presence of a preferred carbon source such as glucose (PubMed:12477937, PubMed:17597928, PubMed:19236936, PubMed:6458044).
Interaction
Subunit
Homododecamer. Adopts a ring-like structure, composed of an arrangement of two hexameric rings stacked on top of one another.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length173
- Mass (Da)18,272
- Last updated1989-10-01 v2
- Checksum6A6EC7594DD46F1B
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 25-29 | in Ref. 3; CAA24237 | ||||
Sequence: IYGST → STAQS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X14603 EMBL· GenBank· DDBJ | CAA32749.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
V00869 EMBL· GenBank· DDBJ | CAA24237.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CM002242 EMBL· GenBank· DDBJ | EAA30377.1 EMBL· GenBank· DDBJ | Genomic DNA |