Q5AD27
Gene name |
TAH18 |
Protein name |
NADPH-dependent diflavin oxidoreductase 1 |
Names |
NADPH-dependent FMN and FAD-containing oxidoreductase |
Species |
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
KEGG Pathway |
cal:CAALFM_C200840WA |
EC number |
|
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 Q5AD27
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5AD27-F1 | Predicted | AlphaFoldDB |
No variants for Q5AD27
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5AD27 | |||||
No associated diseases with Q5AD27
14 regional properties for Q5AD27
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Flavodoxin-like | 6 - 19 | IPR001094-1 |
| domain | Flavodoxin-like | 56 - 67 | IPR001094-2 |
| domain | Flavodoxin-like | 90 - 100 | IPR001094-3 |
| domain | Flavodoxin-like | 114 - 133 | IPR001094-4 |
| domain | Oxidoreductase FAD/NAD(P)-binding | 447 - 548 | IPR001433 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 236 - 246 | IPR001709-1 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 380 - 387 | IPR001709-2 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 412 - 421 | IPR001709-3 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 446 - 465 | IPR001709-4 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 471 - 480 | IPR001709-5 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 538 - 546 | IPR001709-6 |
| domain | Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding | 209 - 417 | IPR003097 |
| domain | Flavodoxin/nitric oxide synthase | 5 - 151 | IPR008254 |
| domain | FAD-binding domain, ferredoxin reductase-type | 202 - 439 | IPR017927 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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. |
| FMN binding | Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. |
| NADP binding | Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. |
| NADPH-hemoprotein reductase activity | Catalysis of the reaction: NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein. |
| 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 |
|---|---|
| iron-sulfur cluster assembly | The incorporation of iron and exogenous sulfur into a metallo-sulfur cluster. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTGEITILYG | SETGNAEEYA | KYLKQRLRSY | NLKPINLASL | DDYPLKRLVT | HTSYLIIICS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TTGQGEIPRN | GKKFMKFILK | KKLPSDLFQH | LQLTTFGVGD | SSYVKYNYAI | KKIHTRLMQL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GCQLLSPRCE | ADEISPEGVD | GYYIEWEAEL | IAALLNKFPS | ASKISSEAVP | MPEYRISVSK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SDTTIDPKEV | IDNPIVSRLG | KDGLKLGTVL | ENNRLTSSNH | FQDVRDFKFS | SNGLNYLPGD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TVSLFPCNFD | EDVDALLQSQ | PQWLKIADKP | LNLKNFPHLE | GGFADILTLR | TLFKYHLDIM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SIPRRSFFAL | LWHFVDPSTE | DGEREQEKLK | EFGSLDEPEE | LYDYANRPRR | SILETLLEFE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NNLTIPVSYI | LDLFPLIRPR | MFSIASCPSS | KEVELVVAIV | EYKTIIRKIR | RGVCTRWLKN |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LKPGDQFLFS | IQRSSFKYKD | DNSPIIMVAP | GTGIAPMKSL | IDEVIQNNSK | QELYLFFGCR |
| 490 | 500 | 510 | 520 | 530 | 540 |
| FKEKDNLIES | FWHGNENQNL | HLVSAYSRDS | NSKYRYVQDA | LFAHSELIGK | LLIEQNAKVF |
| 550 | 560 | 570 | 580 | ||
| VCGSSGKMPR | EVKITFVEIV | KKFTGMDEGD | AQKYIIGLED | NGRYKEDAW |