A1KLN4 (AROQ_MYCBP) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 46.
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: 3-dehydroquinate dehydratase Short name=3-dehydroquinase EC=4.2.1.10 Alternative name(s): Type II DHQase | ||||
| Gene names |
| ||||
| Organism | Mycobacterium bovis (strain BCG / Pasteur 1173P2) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 410289 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › ![]() |
Protein attributes
| Sequence length | 147 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes a trans-dehydration via an enolate intermediate By similarity. HAMAP-Rule MF_00169 |
| Catalytic activity | 3-dehydroquinate = 3-dehydroshikimate + H2O. HAMAP-Rule MF_00169 |
| Pathway | Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. HAMAP-Rule MF_00169 |
| Subunit structure | Homododecamer By similarity. |
| Sequence similarities | Belongs to the type-II 3-dehydroquinase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Aromatic amino acid biosynthesis |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: HAMAP chorismate biosynthetic processInferred from electronic annotation. Source: UniProtKB-UniPathway |
| 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 – 147 | 147 | 3-dehydroquinate dehydratase HAMAP-Rule MF_00169 | PRO_1000023487 | |||||
Regions | |||||||||
| Region | 103 – 104 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 25 | 1 | Proton acceptor By similarity | ||||||
| Active site | 102 | 1 | Proton donor By similarity | ||||||
| Binding site | 76 | 1 | Substrate By similarity | ||||||
| Binding site | 82 | 1 | Substrate By similarity | ||||||
| Binding site | 89 | 1 | Substrate By similarity | ||||||
| Binding site | 113 | 1 | Substrate By similarity | ||||||
| Site | 20 | 1 | Transition state stabilizer By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Genome plasticity of BCG and impact on vaccine efficacy." Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T. Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BCG / Pasteur 1173P2. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM408590 Genomic DNA. Translation: CAL72547.1. |
| RefSeq | YP_978645.1. NC_008769.1. |
3D structure databases | |
| ProteinModelPortal | A1KLN4. |
| SMR | A1KLN4. Positions 1-144. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 410289.BCG_2559c. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAL72547; CAL72547; BCG_2559c. |
| GeneID | 4699191. |
| KEGG | mbb:BCG_2559c. |
| PATRIC | 18016095. VBIMycBov80988_2798. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0757. |
| HOGENOM | HOG000217278. |
| KO | K03786. |
| OMA | EPDVYGA. |
| ProtClustDB | PRK05395. |
Enzyme and pathway databases | |
| BioCyc | MBOV410289:GJW7-2595-MONOMER. |
| UniPathway | UPA00053; UER00086. |
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... |
Other | |
| BindingDB | A1KLN4. |
Entry information
| Entry name | AROQ_MYCBP | ||||||||
| Accession | Primary (citable) accession number: A1KLN4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
