Q8HXW0
Gene name |
GULO |
Protein name |
L-gulonolactone oxidase |
Names |
LGO, L-gulono-gamma-lactone oxidase, GLO |
Species |
Sus scrofa (Pig) |
KEGG Pathway |
ssc:396759 |
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 Q8HXW0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8HXW0-F1 | Predicted | AlphaFoldDB |
5 variants for Q8HXW0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3476703540 | 121 | V>F | No | EVA | |
| rs338494236 | 154 | V>L | No | EVA | |
| rs701473535 | 197 | S>T | No | EVA | |
| rs345987267 | 258 | F>L | No | EVA | |
| rs712059675 | 320 | L>I | No | EVA |
No associated diseases with Q8HXW0
1 regional properties for Q8HXW0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| active_site | Lipase, GDSL, active site | 38 - 49 | IPR008265 |
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 |
| P58710 | Gulo | L-gulonolactone oxidase | Mus musculus (Mouse) | 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 |
| MVHGHKGVKF | QNWAKTYGCC | PEMYYQPTSV | EEIREVLALA | RQQNKRVKVV | GGGHSPSDIA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| CTDGFMIHMG | KMNRVLKVDM | EKKQVTVEAG | ILLADLHPQL | DKHGLALSNL | GAVSDVTAGG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VIGSGTHNTG | IKHGILATQV | VELTLLTPDG | TVLVCSESSN | AEVFQAARVH | LGCLGVILTV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TLQCVPQFHL | QETTFPSTLK | EVLDNLDSHL | KKSEYFRFLW | FPHSENVSVI | YQDHTNKPPS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SSANWFWDYA | IGFYLLEFLL | WISTFVPGLV | GWINRFFFWL | LFNGKKENCN | LSHKIFTYEC |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RFKQHVQDWA | IPREKTKEAL | LELKAMLEAH | PKVVAHYPVE | VRFTRADDIL | LSPCFQRDSC |
| 370 | 380 | 390 | 400 | 410 | 420 |
| YMNIIMYRPY | GKDVPRLDYW | LAYETIMKKV | GGRPHWAKAH | NCTRKDFEKM | YPAFRKFCAI |
| 430 | |||||
| REKLDPTGMF | LNAYLEKVFY |