Q0P5F9
Gene name |
ALDH8A1 |
Protein name |
2-aminomuconic semialdehyde dehydrogenase |
Names |
Aldehyde dehydrogenase family 8 member A1 |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:513537 |
EC number |
1.2.1.32: 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 Q0P5F9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q0P5F9-F1 | Predicted | AlphaFoldDB |
No variants for Q0P5F9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q0P5F9 | |||||
No associated diseases with Q0P5F9
1 regional properties for Q0P5F9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Anoctamin, dimerisation domain | 108 - 332 | IPR032394 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.2.1.32 | With NAD(+) or NADP(+) as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| aminomuconate-semialdehyde dehydrogenase activity | Catalysis of the reaction: H2O + NAD+ + 2-aminomuconate semialdehyde = NADH + 2-amino-muconate. |
| oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor | Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces NAD or NADP. |
| retinal dehydrogenase activity | Catalysis of the reaction: retinal + NAD+ + H2O = retinoate + NADH. Acts on both 11-trans and 13-cis forms of retinal. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| L-kynurenine catabolic process | The chemical reactions and pathways resulting in the breakdown of L-kynurenine, the L-enantiomer of the amino acid kynurenine (3-(2-aminobenzoyl)-alanine). |
| retinal metabolic process | The chemical reactions and pathways involving retinal, a compound that plays an important role in the visual process in most vertebrates. In the retina, retinal combines with opsins to form visual pigments. Retinal is one of the forms of vitamin A. |
| retinoic acid metabolic process | The chemical reactions and pathways involving retinoic acid, one of the three components that makes up vitamin A. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P05091 | ALDH2 | Aldehyde dehydrogenase, mitochondrial | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAGRGGLLML | ENFIGGKFLP | CSSYLDSYDP | STGEVYCHVP | NSGKEEIEAA | VEAARAAFPG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| WSSRSPQERS | QVLQRLADLL | EQSLEELAQA | ESKDQGKTIT | LARTMDIPRA | VHNFRFFASS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ILHHTSECTQ | MDHLGCLHYT | VRAPVGIAAL | ISPWNLPLYL | LTWKIAPAIA | AGNTVIAKPS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ELTSVTAWMM | CRLLEKAGVP | PGVVNIVFGT | GPRVGEALVS | HPEVPLISFT | GSQPTAERIM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QLSAPHCKKL | SLELGGKNPA | VIFEDANLAE | CIPTTVRSSF | ANQGEICLCT | SRIFVQRSIY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SEFLKRFVEA | ARMWKVGIPS | DPSADMGALI | SKAHLEKVRS | YIKKARMEGA | QILCGEGVDK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LNLPPRNQAG | YFMLPTVITD | VKDESCCMKE | EIFGPVTCVV | PFDSEEEVIQ | RANNVKYGLA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ATVWSGNVGR | VHRVAKKLQS | GLVWTNCWLI | RELNLPFGGM | KSSGVGREGA | KDSYEFFTEV |
| KTITVKH |