Q5E9N4
Gene name |
AADAT |
Protein name |
Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial |
Names |
KAT/AadAT, 2-aminoadipate aminotransferase, 2-aminoadipate transaminase, Alpha-aminoadipate aminotransferase, AadAT, Glycine transaminase AADAT, Kynurenine aminotransferase II, Kynurenine--glyoxylate transaminase AADAT, Kynurenine--oxoglutarate aminotransferase II, Kynurenine--oxoglutarate transaminase 2, Kynurenine--oxoglutarate transaminase II, Methionine--glyoxylate transaminase AADAT |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:508929 |
EC number |
2.6.1.4: Transaminases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q5E9N4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5E9N4-F1 | Predicted | AlphaFoldDB |
No variants for Q5E9N4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5E9N4 | |||||
No associated diseases with Q5E9N4
Functions
| Description | ||
|---|---|---|
| EC Number | 2.6.1.4 | Transaminases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| 2-aminoadipate transaminase activity | Catalysis of the reaction: 2-oxoglutarate + L-2-aminoadipate = 2-oxoadipate + L-glutamate. |
| glycine:2-oxoglutarate aminotransferase activity | Catalysis of the reaction: glycine + 2-oxoglutarate = glyoxylate + L-glutamate. |
| kynurenine-glyoxylate transaminase activity | Catalysis of the reaction: L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine. |
| kynurenine-oxoglutarate transaminase activity | Catalysis of the reaction: L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate. |
| methionine-glyoxylate transaminase activity | Catalysis of the reaction: L-methionine + glyoxylate = 4-methylthio-2-oxobutanoate + glycine. |
| pyridoxal phosphate binding | Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. |
| transaminase activity | Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| 2-oxoglutarate metabolic process | The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism. |
| alpha-amino acid metabolic process | The chemical reactions and pathways involving an alpha-amino acid. |
| biosynthetic process | The chemical reactions and pathways resulting in the formation of substances; typically the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones. |
| glutamate metabolic process | The chemical reactions and pathways involving glutamate, the anion of 2-aminopentanedioic acid. |
| kynurenine metabolic process | The chemical reactions and pathways involving kynurenine, the amino acid 3-(2-aminobenzoyl)-alanine. |
| L-lysine catabolic process to acetyl-CoA via saccharopine | The chemical reactions and pathways resulting in the breakdown of L-lysine into other compounds, including acetyl-CoA, via the intermediate saccharopine. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNYARFITAT | SAARKPSTIR | VMTEILSKAP | KSVISLATGA | PNPNTFPFKT | AVITIENGKP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IQFNEQMMKR | ALQYSQSAGI | PELLSWLKQL | QVKLHNPPTI | HYAPTQGQMD | LCVTCGSQEG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LCKVFEMIVN | PGDNILVNEP | IYSGTIHALQ | PLGCNMINVS | SDEHGIIPDS | LREILSKWKP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EDSKNPKKNS | PKFLYTVPNG | NNPSGNSLTA | ERKREIYELA | RKYDFLIIED | DPYYFMQFNK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PWAPTFLSMD | EDGRVIRADS | FSKVLSSGLR | IGFITGPKPL | IERIVLHIQV | STMHPSTFAQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LLVSQLLYQW | GEEGFLGHVD | RVIDFYRKQR | DALMAAADKW | LSGLAEWHVP | TAGMFLWVKI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KGIHDVRKLI | EEKAFKKEIF | MLPGCGFYTD | SSAPCPYFRA | SFSSASPEQM | DLAFQRLAQL |
| IKESL |