A3LYE4 (3DHQ_PICST) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 43.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Catabolic 3-dehydroquinase Short name=cDHQase EC=4.2.1.10 Alternative name(s): 3-dehydroquinate dehydratase | ||||
| Gene names |
| ||||
| Organism | Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545) (Yeast) (Pichia stipitis) [Complete proteome] | ||||
| Taxonomic identifier | 322104 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Scheffersomyces › ![]() |
Protein attributes
| Sequence length | 146 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Is involved in the catabolism of quinate. Allows the utilization of quinate as carbon source via the beta-ketoadipate pathway By similarity. HAMAP-Rule MF_03136 |
| Catalytic activity | 3-dehydroquinate = 3-dehydroshikimate + H2O. HAMAP-Rule MF_03136 |
| Pathway | Aromatic compound metabolism; 3,4-dihydroxybenzoate biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 1/2. HAMAP-Rule MF_03136 |
| Subunit structure | Homododecamer By similarity. Adopts a ring-like structure, composed of an arrangement of two hexameric rings stacked on top of one another By similarity. HAMAP-Rule MF_03136 |
| Sequence similarities | Belongs to the type-II 3-dehydroquinase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Quinate metabolism |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | quinate metabolic process Inferred from electronic annotation. Source: HAMAP |
| Molecular_function | 3-dehydroquinate dehydratase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 146 | 146 | Catabolic 3-dehydroquinase HAMAP-Rule MF_03136 | PRO_0000402375 | |||||
Regions | |||||||||
| Region | 105 – 106 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 24 | 1 | Proton acceptor By similarity | ||||||
| Active site | 104 | 1 | Proton donor By similarity | ||||||
| Binding site | 78 | 1 | Substrate By similarity | ||||||
| Binding site | 84 | 1 | Substrate By similarity | ||||||
| Binding site | 91 | 1 | Substrate By similarity | ||||||
| Binding site | 115 | 1 | Substrate By similarity | ||||||
| Site | 19 | 1 | Transition state stabilizer By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting yeast Pichia stipitis." Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., Passoth V., Richardson P.M. Nat. Biotechnol. 25:319-326(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000500 Genomic DNA. Translation: ABN67969.1. |
| RefSeq | XP_001385998.1. XM_001385961.1. |
3D structure databases | |
| ProteinModelPortal | A3LYE4. |
| SMR | A3LYE4. Positions 2-145. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 4924.PICST_62322. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4840232. |
| KEGG | pic:PICST_62322. |
Phylogenomic databases | |
| eggNOG | COG0757. |
| HOGENOM | HOG000217278. |
| KO | K03786. |
| OMA | RREPGHY. |
| OrthoDB | EOG4W6S5K. |
Enzyme and pathway databases | |
| UniPathway | UPA00088; UER00178. |
Family and domain databases | |
| Gene3D | 3.40.50.9100. 1 hit. |
| HAMAP | MF_00169. AroQ. |
| InterPro | IPR001874. DHquinase_II. IPR018509. DHquinase_II_CS. [Graphical view] |
| PANTHER | PTHR21272. PTHR21272. 1 hit. |
| Pfam | PF01220. DHquinase_II. 1 hit. [Graphical view] |
| PIRSF | PIRSF001399. DHquinase_II. 1 hit. |
| ProDom | PD004527. DHquinase_II. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SUPFAM | SSF52304. DHquinase_II. 1 hit. |
| TIGRFAMs | TIGR01088. aroQ. 1 hit. |
| PROSITE | PS01029. DEHYDROQUINASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | 3DHQ_PICST | ||||||||
| Accession | Primary (citable) accession number: A3LYE4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
