Q78JT3
Gene name |
Haao |
Protein name |
3-hydroxyanthranilate 3,4-dioxygenase |
Names |
3-hydroxyanthranilate oxygenase, 3-HAO, 3-hydroxyanthranilic acid dioxygenase, HAD |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:107766 |
EC number |
1.13.11.6: With incorporation of two atoms of oxygen |
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 Q78JT3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q78JT3-F1 | Predicted | AlphaFoldDB |
11 variants for Q78JT3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs234856061 | 2 | E>D | No | EVA | |
| rs3389451169 | 26 | L>P | No | EVA | |
| rs3389484441 | 63 | I>K | No | EVA | |
| rs3389441944 | 108 | R>L | No | EVA | |
| rs3389484453 | 141 | L>I | No | EVA | |
| rs3389476178 | 192 | R>K | No | EVA | |
| rs3389484382 | 245 | C>S | No | EVA | |
| rs3389473730 | 255 | L>P | No | EVA | |
| rs231496917 | 259 | G>R | No | EVA | |
| rs3389483183 | 260 | T>S | No | EVA | |
| rs3389489702 | 269 | G>C | No | EVA |
No associated diseases with Q78JT3
No regional properties for Q78JT3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q78JT3 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 1.13.11.6 | With incorporation of two atoms of oxygen |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| mitochondrial membrane | Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| 3-hydroxyanthranilate 3,4-dioxygenase activity | Catalysis of the reaction: 3-hydroxyanthranilate + O(2) = cis,cis-2-amino-3-(3-oxoprop-1-enyl)but-2-enedioate + H(+). |
| ferrous iron binding | Binding to a ferrous iron ion, Fe(II). |
| iron ion binding | Binding to an iron (Fe) ion. |
| oxygen binding | Binding to oxygen (O2). |
9 GO annotations of biological process
| Name | Definition |
|---|---|
| 'de novo' NAD biosynthetic process from tryptophan | The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD), beginning with the synthesis of tryptophan from simpler precursors; biosynthesis may be of either the oxidized form, NAD, or the reduced form, NADH. |
| anthranilate metabolic process | The chemical reactions and pathways involving anthranilate (2-aminobenzoate). |
| NAD biosynthetic process | The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide, a coenzyme present in most living cells and derived from the B vitamin nicotinic acid; biosynthesis may be of either the oxidized form, NAD, or the reduced form, NADH. |
| neuron cellular homeostasis | The cellular homeostatic process that preserves a neuron in a stable, differentiated functional and structural state. |
| quinolinate biosynthetic process | The chemical reactions and pathways resulting in the formation of quinolinate, the anion of quinolinic acid, also known as 2,3-pyridinedicarboxylic acid. |
| quinolinate metabolic process | The chemical reactions and pathways involving quinolinate, the anion of quinolinic acid, also known as 2,3-pyridinedicarboxylic acid. |
| response to cadmium ion | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cadmium (Cd) ion stimulus. |
| response to zinc ion | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a zinc ion stimulus. |
| tryptophan catabolic process | The chemical reactions and pathways resulting in the breakdown of tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MERRVRVKSW | VEENRASFQP | PVCNKLMHQE | QLKIMFVGGP | NTRKDYHIEE | GEEVFYQLEG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DMILRVLEQG | QHRDVPIRQG | EIFLLPARVP | HSPQRFANTM | GLVIERRRLE | SELDGLRYYV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GDTEDVLFEK | WFHCKDLGTQ | LAPIIQEFFH | SEQYRTGKPN | PDQLLKELPF | PLNTRSIMKP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| MSLKAWLDGH | SRELQAGTSL | SLFGDSYETQ | VIAHGQGSSK | GPRQDVDVWL | WQQEGSSKVT |
| 250 | 260 | 270 | 280 | ||
| MGGQCIALAP | DDSLLVPAGT | SYVWERAQGS | VALSVTQDPA | RKKPWW |