Reviewed,
UniProtKB/Swiss-Prot A2S5J7 (DAPB_BURM9)
Last modified
June 16, 2009.
Version 18.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Dihydrodipicolinate reductase Short name=DHPR EC=1.3.1.26 | ||||
| Gene names |
| ||||
| Organism | Burkholderia mallei (strain NCTC 10229) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 412022 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group |
Protein attributes
| Sequence length | 268 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | 2,3,4,5-tetrahydrodipicolinate + NAD(P)+ = 2,3-dihydrodipicolinate + NAD(P)H. HAMAP MF_00102 |
| Pathway | Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; tetrahydrodipicolinate from L-aspartate: step 4/4. HAMAP MF_00102 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the dihydrodipicolinate reductase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | diaminopimelate biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | binding Inferred from electronic annotation. Source: InterPro dihydrodipicolinate reductase 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 – 268 | 268 | Dihydrodipicolinate reductase HAMAP MF_00102 | PRO_1000008543 | |||
Sequences
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References
| [1] | DeShazer D., Woods D.E., Nierman W.C. Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000546 Genomic DNA. Translation: ABN02151.1. | |
| RefSeq | YP_001027216.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 4790988. |
| GenomeReviews | Gene locus BMA10229_A1232 in contig CP000546_GR. |
| KEGG | bml:BMA10229_A1232. |
| TIGR | BMA10229_A1232. |
Phylogenomic databases | |
| OMA | A2S5J7. TIGFSTI. |
Family and domain databases | |
| HAMAP | MF_00102. [Tree] |
| InterPro | IPR000846. DapB. IPR011770. DapB_bac/pln. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 2 hits. |
| PANTHER | PTHR20836. DapB_bac/pln. 1 hit. |
| Pfam | PF05173. DapB_C. 1 hit. PF01113. DapB_N. 1 hit. [Graphical view] |
| ProDom | PD004105. DapB. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR00036. dapB. 1 hit. |
| PROSITE | PS01298. DAPB. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DAPB_BURM9 | ||||||||
| Accession | Primary (citable) accession number: A2S5J7 | ||||||||
| 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


