Q64602 (AADAT_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 94.
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: Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial Short name=KAT/AadAT Alternative name(s): 2-aminoadipate aminotransferase 2-aminoadipate transaminase EC=2.6.1.39 Alpha-aminoadipate aminotransferase Short name=AadAT Kynurenine aminotransferase II Kynurenine--oxoglutarate aminotransferase II Kynurenine--oxoglutarate transaminase 2 EC=2.6.1.7 Kynurenine--oxoglutarate transaminase II | ||||
| Gene names |
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| 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 | 425 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro) By similarity. |
| Catalytic activity | L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate. L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate. |
| Cofactor | Pyridoxal phosphate. |
| Pathway | |
| Subunit structure | Homodimer. Ref.1 |
| Subcellular location | Mitochondrion Potential. |
| Post-translational modification | The N-terminus is blocked. |
| Sequence similarities | Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 29 | 29 | Mitochondrion Potential | ||||||
| Chain | 30 – 425 | 396 | Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial | PRO_0000020604 | |||||
Sites | |||||||||
| Binding site | 20 | 1 | Substrate By similarity | ||||||
| Binding site | 74 | 1 | Substrate By similarity | ||||||
| Binding site | 142 | 1 | Substrate By similarity | ||||||
| Binding site | 202 | 1 | Substrate By similarity | ||||||
| Binding site | 399 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 263 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and functional expression of a soluble form of kynurenine/alpha-aminoadipate aminotransferase from rat kidney." Buchli R., Alberati-Giani D., Malherbe P., Koehler C., Broger C., Cesura A.M. J. Biol. Chem. 270:29330-29335(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], HOMODIMERIZATION, PARTIAL PROTEIN SEQUENCE. Tissue: Kidney. |
| [2] | "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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z50144 mRNA. Translation: CAA90507.1. BC078864 mRNA. Translation: AAH78864.1. |
| IPI | IPI00214373. |
| RefSeq | NP_058889.1. NM_017193.1. |
| UniGene | Rn.11133. |
3D structure databases | |
| ProteinModelPortal | Q64602. |
| SMR | Q64602. Positions 1-423. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10116.ENSRNOP00000015974. |
PTM databases | |
| PhosphoSite | Q64602. |
Proteomic databases | |
| PaxDb | Q64602. |
| PRIDE | Q64602. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOT00000015974; ENSRNOP00000015974; ENSRNOG00000011861. |
| GeneID | 29416. |
| KEGG | rno:29416. |
| UCSC | RGD:2948. rat. |
Organism-specific databases | |
| CTD | 51166. |
| RGD | 2948. Aadat. |
Phylogenomic databases | |
| eggNOG | COG1167. |
| GeneTree | ENSGT00390000004594. |
| HOGENOM | HOG000223057. |
| HOVERGEN | HBG050429. |
| InParanoid | Q64602. |
| KO | K00825. |
| OMA | PFQSASI. |
| OrthoDB | EOG480HWQ. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-12251. |
| BRENDA | 2.6.1.7. 5301. |
| SABIO-RK | Q64602. |
| UniPathway | UPA00868; UER00838. |
Gene expression databases | |
| Genevestigator | Q64602. |
| GermOnline | ENSRNOG00000011861. Rattus norvegicus. |
Family and domain databases | |
| Gene3D | 3.40.640.10. 1 hit. 3.90.1150.10. 1 hit. |
| InterPro | IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view] |
| Pfam | PF00155. Aminotran_1_2. 1 hit. [Graphical view] |
| SUPFAM | SSF53383. PyrdxlP-dep_Trfase_major. 1 hit. |
| ProtoNet | Search... |
Other | |
| BindingDB | Q64602. |
| ChEMBL | CHEMBL2662. |
| NextBio | 609096. |
Entry information
| Entry name | AADAT_RAT | ||||||||
| Accession | Primary (citable) accession number: Q64602 | ||||||||
| 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
