Q5RF00
Gene name |
ALDH2 |
Protein name |
Aldehyde dehydrogenase, mitochondrial |
Names |
ALDH class 2, ALDH-E2 |
Species |
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
KEGG Pathway |
pon:100171596 |
EC number |
1.2.1.3: With NAD(+) or NADP(+) as acceptor |
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 Q5RF00
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5RF00-F1 | Predicted | AlphaFoldDB |
No variants for Q5RF00
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5RF00 | |||||
No associated diseases with Q5RF00
No regional properties for Q5RF00
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q5RF00 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 1.2.1.3 | With NAD(+) or NADP(+) as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrial matrix | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. |
| 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. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| aldehyde dehydrogenase (NAD+) activity | Catalysis of the reaction: an aldehyde + NAD+ + H2O = an acid + NADH + H+. |
| carboxylic ester hydrolase activity | Catalysis of the hydrolysis of a carboxylic ester bond. |
| glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity | Catalysis of the reaction: D-glyceraldehyde 3-phosphate + NAD+ + H2O = 3-phospho-D-glycerate + NADH + H+. |
| nitroglycerin reductase activity | Catalysis of the removal of one or more nitrite (NO2-) groups from nitroglycerin or a derivative. |
| phenylacetaldehyde dehydrogenase activity | Catalysis of the reaction: phenylacetaldehyde + NAD+ + H2O = phenylacetate + NADH + H+. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| aldehyde catabolic process | The chemical reactions and pathways resulting in the breakdown of aldehydes, any organic compound with the formula R-CH=O. |
| regulation of dopamine biosynthetic process | Any process that modulates the frequency, rate or extent of dopamine biosynthetic process. |
| regulation of serotonin biosynthetic process | Any process that modulates the frequency, rate or extent of serotonin biosynthetic process. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLRAAARFGP | RLGRRLLSAA | ATQAVPAPNQ | QPEVFCNQIF | INNEWHDAVS | RKTFPTVNPS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TGEVICQVAE | GDKEDVDKAV | KAARAAFQLG | SPWRRMDASH | RGRLLNRLAD | LIERDRTYLA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ALETLDNGKP | YVISYLVDLD | MVLKCLRYYA | GWADKYHGKT | IPIDGDFFSY | TRHEPVGVCG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QIIPWNFPLL | MQAWKLGPAL | ATGNVVVMKV | AEQTPLTALY | VANLIKEAGF | PPGVVNIVPG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FGPTAGAAIA | SHEDVDKVAF | TGSTEIGRVI | QVAAGSSNLK | RVTLELGGKS | PNIIMSDADM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DWAVEQAHFA | LFFNQGQCCC | AGSRTFVQED | IYDEFVERSV | ARAKSRVVGN | PFDSKTEQGP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QVDETQFKKI | LGYINTGKQE | GAKLLCGGGI | AADRGYFIQP | TVFGDVQDGM | TIAKEEIFGP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VMQILKFKTI | EEVVGRANNS | TYGLAAAVFT | KDLDKANYLS | QALQAGTVWV | NCYNVFGAQS |
| 490 | 500 | 510 | |||
| PFGGYKMSGS | GRELGEYGLQ | AYTEVKTVTV | KVPQKNS |