A2VCW9 (AASS_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 48.
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: Alpha-aminoadipic semialdehyde synthase, mitochondrial Alternative name(s): LKR/SDH | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 926 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Bifunctional enzyme that catalyzes the first two steps in lysine degradation. The N-terminal and the C-terminal contain lysine-oxoglutarate reductase and saccharopine dehydrogenase activity, respectively By similarity. UniProtKB Q9UDR5 |
| Catalytic activity | N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-lysine + 2-oxoglutarate + NADPH. UniProtKB Q9UDR5 N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADH. UniProtKB Q9UDR5 |
| Pathway | |
| Subunit structure | Homodimer By similarity. UniProtKB Q9UDR5 |
| Subcellular location | Mitochondrion By similarity UniProtKB Q9UDR5. |
| Sequence similarities | In the N-terminal section; belongs to the AlaDH/PNT family. In the C-terminal section; belongs to the saccharopine dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | NAD NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Multifunctional enzyme Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | L-lysine catabolic process to acetyl-CoA via saccharopine Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Cellular_component | mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity Inferred from electronic annotation. Source: EC saccharopine dehydrogenase (NADP+, L-lysine-forming) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 32 | 32 | Mitochondrion By similarity UniProtKB Q9UDR5 | ||||||
| Chain | 33 – 926 | 894 | Alpha-aminoadipic semialdehyde synthase, mitochondrial UniProtKB Q9UDR5 | PRO_0000315868 | |||||
Regions | |||||||||
| Region | 33 – 455 | 423 | Lysine-ketoglutarate reductase By similarity UniProtKB Q9UDR5 | ||||||
| Region | 477 – 926 | 450 | Saccharopine dehydrogenase By similarity UniProtKB Q9UDR5 | ||||||
Sequences
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References
| [1] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC128771 mRNA. Translation: AAI28772.1. |
| IPI | IPI00858395. |
| RefSeq | NP_001094433.1. NM_001100963.1. |
| UniGene | Rn.198671. |
3D structure databases | |
| ProteinModelPortal | A2VCW9. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10116.ENSRNOP00000057271. |
Proteomic databases | |
| PaxDb | A2VCW9. |
| PRIDE | A2VCW9. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 296925. |
| KEGG | rno:296925. |
| UCSC | RGD:1310811. rat. |
Organism-specific databases | |
| CTD | 10157. |
| RGD | 1310811. Aass. |
Phylogenomic databases | |
| eggNOG | COG1748. |
| HOVERGEN | HBG048688. |
| KO | K14157. |
Enzyme and pathway databases | |
| UniPathway | UPA00868; UER00835. UPA00868; UER00836. |
Gene expression databases | |
| Genevestigator | A2VCW9. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. |
| InterPro | IPR007886. AlaDH/PNT_N. IPR007698. AlaDH/PNT_NAD(H)-bd. IPR016040. NAD(P)-bd_dom. IPR005097. Saccharopine_DH/HSpermid_syn. [Graphical view] |
| Pfam | PF01262. AlaDh_PNT_C. 1 hit. PF05222. AlaDh_PNT_N. 1 hit. PF03435. Saccharop_dh. 1 hit. [Graphical view] |
| SMART | SM01002. AlaDh_PNT_C. 1 hit. SM01003. AlaDh_PNT_N. 1 hit. [Graphical view] |
| PROSITE | PS00836. ALADH_PNT_1. False negative. PS00837. ALADH_PNT_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 641904. |
Entry information
| Entry name | AASS_RAT | ||||||||
| Accession | Primary (citable) accession number: A2VCW9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
