HAMAP rule MF_03136
General rule information
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| Accession | MF_03136 |
| Dates | 22-OCT-2010 (Created)
7-DEC-2023 (Last updated, Version 9) |
| Name | qutE |
| Scope(s) |
Eukaryota Fungi |
| Template(s) | P05147 (3DHQ_EMENI); [ Recover all ] |
| Triggered by |
case c? <OC:Eukaryota>
HAMAP; MF_00169 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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| Identifier | 3DHQ |
| Protein name | RecName: Full=Catabolic 3-dehydroquinase; Short=cDHQase; EC=4.2.1.10; AltName: Full=3-dehydroquinate dehydratase; |
| case <OC:Pezizomycotina> and not <OC:Neurospora> | |
| Gene name | Name=qutE; |
| else case <OC:Neurospora> | |
| Gene name | Name=qa-2; |
| else case <OC:Saccharomycotina> | |
| Gene name | Name=DQD1; |
| end case | |
Comments
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| FUNCTION | Is involved in the catabolism of quinate. Allows the utilization of quinate as carbon source via the beta-ketoadipate pathway. |
| CATALYTIC ACTIVITY | Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; |
| PATHWAY | Aromatic compound metabolism; 3,4-dihydroxybenzoate biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 1/2. |
| SUBUNIT | Homododecamer. Adopts a ring-like structure, composed of an arrangement of two hexameric rings stacked on top of one another. |
| SIMILARITY | Belongs to the type-II 3-dehydroquinase family. |
Keywords
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Gene Ontology
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| GO:0003855; Molecular function:3-dehydroquinate dehydratase activity |
| GO:0019630; Biological process:quinate metabolic process |
Cross-references
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| Pfam | PF01220; DHquinase_II; 1; |
| NCBIfam | TIGR01088; AroQ; 1; |
| PIRSF | PIRSF001399; DHquinase_II; 1; |
| PROSITE | PS01029; DEHYDROQUINASE_II; 1; |
Features
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| From: 3DHQ_EMENI (P05147) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 102 | 103 | /ligand="substrate" | [IV]-[ST] | ||||||||
| ACT_SITE | 24 | 24 | /note="Proton acceptor" | Y | ||||||||
| ACT_SITE | 101 | 101 | /note="Proton donor" | H | ||||||||
| BINDING | 75 | 75 | /ligand="substrate" | N | ||||||||
| BINDING | 81 | 81 | /ligand="substrate" | H | ||||||||
| BINDING | 88 | 88 | /ligand="substrate" | D | ||||||||
| BINDING | 112 | 112 | /ligand="substrate" | R | ||||||||
| SITE | 19 | 19 | /note="Transition state stabilizer" | R | ||||||||
Additional information
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| Size range | 144-175 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |