Q3ZC33
Gene name |
GULO |
Protein name |
L-gulonolactone oxidase |
Names |
LGO, L-gulono-gamma-lactone oxidase, GLO |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:286812 |
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 Q3ZC33
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q3ZC33-F1 | Predicted | AlphaFoldDB |
58 variants for Q3ZC33
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs444247689 | 36 | V>A | No | EVA | |
| rs444247689 | 36 | V>G | No | EVA | |
| rs3423270410 | 64 | G>S | No | EVA | |
| rs474739878 | 73 | N>T | No | EVA | |
| rs440110540 | 74 | R>P | No | EVA | |
| rs442926088 | 97 | H>P | No | EVA | |
| rs459812486 | 99 | Q>H | No | EVA | |
| rs479875490 | 105 | L>Q | No | EVA | |
| rs442619002 | 112 | A>D | No | EVA | |
| rs459534233 | 116 | V>G | No | EVA | |
| rs438508531 | 133 | H>R | No | EVA | |
| rs458545681 | 134 | G>A | No | EVA | |
| rs468366601 | 140 | V>A | No | EVA | |
| rs468366601 | 140 | V>G | No | EVA | |
| rs718115122 | 149 | N>S | No | EVA | |
| rs464214657 | 158 | S>A | No | EVA | |
| rs432790009 | 164 | F>Y | No | EVA | |
| rs455964447 | 179 | T>A | No | EVA | |
| rs476744829 | 189 | H>R | No | EVA | |
| rs442256682 | 198 | T>P | No | EVA | |
| rs472793936 | 201 | E>A | No | EVA | |
| rs208467135 | 220 | W>R | No | EVA | |
| rs434670338 | 233 | D>A | No | EVA | |
| rs451463527 | 236 | N>T | No | EVA | |
| rs469102728 | 258 | F>L | No | EVA | |
| rs454497410 | 261 | W>L | No | EVA | |
| rs475136762 | 263 | S>I | No | EVA | |
| rs471459263 | 264 | T>I | No | EVA | |
| rs443242183 | 265 | F>Y | No | EVA | |
| rs463342293 | 266 | L>M | No | EVA | |
| rs449614218 | 270 | V>L | No | EVA | |
| rs460030551 | 273 | I>M | No | EVA | |
| rs1116688779 | 283 | N>S | No | EVA | |
| rs476246991 | 287 | E>* | No | EVA | |
| rs454301509 | 317 | K>E | No | EVA | |
| rs464766536 | 317 | K>R | No | EVA | |
| rs464766536 | 317 | K>T | No | EVA | |
| rs433369608 | 318 | E>K | No | EVA | |
| rs442069219 | 344 | T>P | No | EVA | |
| rs455752398 | 349 | I>M | No | EVA | |
| rs472551402 | 350 | L>M | No | EVA | |
| rs440300075 | 350 | L>R | No | EVA | |
| rs460356297 | 351 | L>M | No | EVA | |
| rs439379499 | 358 | D>V | No | EVA | |
| rs462520474 | 360 | C>* | No | EVA | |
| rs482506513 | 363 | N>T | No | EVA | |
| rs448056275 | 368 | R>M | No | EVA | |
| rs445284789 | 394 | P>A | No | EVA | |
| rs465323240 | 395 | H>P | No | EVA | |
| rs472939185 | 400 | H>N | No | EVA | |
| rs432675668 | 400 | H>R | No | EVA | |
| rs452642791 | 401 | N>K | No | EVA | |
| rs444590065 | 405 | K>T | No | EVA | |
| rs461315858 | 406 | D>E | No | EVA | |
| rs208119989 | 411 | Y>* | No | EVA | |
| rs458819154 | 428 | G>A | No | EVA | |
| rs467539229 | 433 | A>V | No | EVA | |
| rs481174816 | 438 | V>E | No | EVA |
No associated diseases with Q3ZC33
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 |
|---|---|---|---|---|
| P58710 | Gulo | L-gulonolactone oxidase | Mus musculus (Mouse) | 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 |
| MVHGYKGVKF | QNWARTYGCC | PEMYFQPTSV | EEVREVLALA | RQQNKRVKVV | GGGHSPSDIA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| CTDGFMIHMG | KMNRVLKVDT | EKKQVTVEAG | ILLADLHPQL | DKHGLALSNL | GAVSDVTAGG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VIGSGTHNTG | IKHGILATQV | VALTLLTANG | TILECSESSN | AEVFQAARVH | LGCLGVILTV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TLQCVPQFHL | QETTFPSTLK | EVLDNLDSHL | KKSEYFRFLW | FPHSENVSVI | YQDHTNKPPS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SSANWFWDYA | IGFYLLEFLL | WISTFLPGLV | GWINRFFFWL | LFNGKKENCN | LSHKIFTYEC |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RFKQHVQDWA | IPREKTKEAL | LELKAMLEAN | PKVVAHYPVE | VRFTRGDDIL | LSPCFQRDSC |
| 370 | 380 | 390 | 400 | 410 | 420 |
| YMNIIMYRPY | GKDVPRLDYW | LAYETIMKKV | GGRPHWAKAH | NCTRKDFEKM | YPAFQRFCAI |
| 430 | |||||
| REKLDPTGMF | LNAYLEKVFY |