P58710
Gene name |
Gulo |
Protein name |
L-gulonolactone oxidase |
Names |
LGO, L-gulono-gamma-lactone oxidase, GLO |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:268756 |
EC number |
1.1.3.8: With oxygen 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 P58710
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P58710-F1 | Predicted | AlphaFoldDB |
20 variants for P58710
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389338034 | 2 | V>* | No | EVA | |
| rs3389292175 | 13 | W>* | No | EVA | |
| rs3389338020 | 56 | P>L | No | EVA | |
| rs3389340607 | 58 | D>Y | No | EVA | |
| rs3389262060 | 90 | G>D | No | EVA | |
| rs3389353476 | 99 | Q>* | No | EVA | |
| rs3389328709 | 119 | G>S | No | EVA | |
| rs3389353477 | 127 | H>Y | No | EVA | |
| rs31067467 | 151 | T>A | No | EVA | |
| rs219467087 | 153 | L>V | No | EVA | |
| rs3389301529 | 203 | L>I | No | EVA | |
| rs3389309848 | 268 | R>E* | No | EVA | |
| rs3389338037 | 270 | V>G | No | EVA | |
| rs3389344521 | 285 | K>N | No | EVA | |
| rs3389342007 | 373 | D>E | No | EVA | |
| rs3389332598 | 429 | M>K | No | EVA | |
| rs3389335370 | 429 | M>L | No | EVA | |
| rs3405211060 | 430 | F>* | No | EVA | |
| rs3404977929 | 441 | Y>L | No | EVA | |
| rs3405301332 | 441 | Y>Y | No | EVA |
No associated diseases with P58710
4 regional properties for P58710
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| binding_site | Oxygen oxidoreductase covalent FAD-binding site | 21 - 54 | IPR006093 |
| domain | FAD linked oxidase, N-terminal | 21 - 156 | IPR006094 |
| domain | D-arabinono-1,4-lactone oxidase, C-terminal domain | 180 - 437 | IPR007173 |
| domain | FAD-binding domain, PCMH-type | 17 - 187 | IPR016166 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.1.3.8 | With oxygen 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 |
|---|---|
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| D-arabinono-1,4-lactone oxidase activity | Catalysis of the reaction: D-arabinono-1,4-lactone + O(2) = dehydro-D-arabinono-1,4-lactone + H(2)O(2) + H(+). |
| FAD binding | Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. |
| flavin adenine dinucleotide binding | Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. |
| L-gulonolactone oxidase activity | Catalysis of the reaction: L-gulono-1,4-lactone + O2 = L-xylo-hex-3-ulonolactone + H2O2. |
| oxidoreductase activity | Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| L-ascorbic acid biosynthetic process | The chemical reactions and pathways resulting in the formation of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions. |
5 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q3ZC33 | GULO | L-gulonolactone oxidase | Bos taurus (Bovine) | PR |
| Q8HXW0 | GULO | L-gulonolactone oxidase | Sus scrofa (Pig) | PR |
| P10867 | Gulo | L-gulonolactone oxidase | Rattus norvegicus (Rat) | PR |
| Q2QXY1 | GLDH2 | L-galactono-1,4-lactone dehydrogenase 2, mitochondrial | Oryza sativa subsp japonica (Rice) | PR |
| Q2RAP0 | GLDH1 | L-galactono-1,4-lactone dehydrogenase 1, mitochondrial | Oryza sativa subsp japonica (Rice) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVHGYKGVQF | QNWAKTYGCS | PEMYYQPTSV | GEVREVLALA | RQQNKKVKVV | GGGHSPSDIA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| CTDGFMIHMG | KMNRVLQVDK | EKKQVTVEAG | ILLTDLHPQL | DKHGLALSNL | GAVSDVTVGG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VIGSGTHNTG | IKHGILATQV | VALTLMKADG | TVLECSESSN | ADVFQAARVH | LGCLGVILTV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TLQCVPQFHL | LETSFPSTLK | EVLDNLDSHL | KKSEYFRFLW | FPHSENVSII | YQDHTNKEPS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SASNWFWDYA | IGFYLLEFLL | WTSTYLPRLV | GWINRFFFWL | LFNCKKESSN | LSHKIFSYEC |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RFKQHVQDWA | IPREKTKEAL | LELKAMLEAH | PKVVAHYPVE | VRFTRGDDIL | LSPCFQRDSC |
| 370 | 380 | 390 | 400 | 410 | 420 |
| YMNIIMYRPY | GKDVPRLDYW | LAYETIMKKF | GGRPHWAKAH | NCTRKDFEKM | YPAFHKFCDI |
| 430 | |||||
| REKLDPTGMF | LNSYLEKVFY |