Reviewed,
UniProtKB/Swiss-Prot A1WBZ2 (AROE_ACISJ)
Last modified
November 3, 2009.
Version 28.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Shikimate dehydrogenase EC=1.1.1.25 | ||||
| Gene names |
| ||||
| Organism | Acidovorax sp. (strain JS42) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 232721 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Acidovorax |
Protein attributes
| Sequence length | 282 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | Shikimate + NADP+ = 3-dehydroshikimate + NADPH. HAMAP MF_00222 |
| Pathway | Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. HAMAP MF_00222 |
| Sequence similarities | Belongs to the shikimate dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Aromatic amino acid biosynthesis |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular function | NADP or NADPH binding Inferred from electronic annotation. Source: InterPro shikimate 5-dehydrogenase activityInferred 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 – 282 | 282 | Shikimate dehydrogenase HAMAP MF_00222 | PRO_0000325092 | |||||
Regions | |||||||||
| Nucleotide binding | 130 – 134 | 5 | NADP By similarity | ||||||
Sites | |||||||||
| Active site | 69 | 1 | Proton acceptor Potential | ||||||
Sequences
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References
| [1] | "Complete sequence of chromosome 1 of Acidovorax sp. JS42." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. Richardson P.Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000539 Genomic DNA. Translation: ABM43767.1. | |
| RefSeq | YP_987843.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A1WBZ2. |
Genome annotation databases | |
| GeneID | 4674125. |
| GenomeReviews | Gene locus Ajs_3656 in contig CP000539_GR. |
| KEGG | ajs:Ajs_3656. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | HGATARD. |
Family and domain databases | |
| HAMAP | MF_00222. [Tree] |
| InterPro | IPR016040. NAD(P)-bd_dom. IPR011342. Quinate/shikimate_5-DH. IPR013708. Shikimate_DH-bd_N. IPR006151. Shikm_DH/Glu-tRNA_Rdtase. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF01488. Shikimate_DH. 1 hit. PF08501. Shikimate_dh_N. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00507. aroE. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | AROE_ACISJ | ||||||||
| Accession | Primary (citable) accession number: A1WBZ2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


