A2AI05
PR
Gene name |
Ndor1 |
Protein name |
NADPH-dependent diflavin oxidoreductase 1 |
Names |
NADPH-dependent FMN and FAD-containing oxidoreductase |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:78797 |
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 A2AI05
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A2AI05-F1 | Predicted | AlphaFoldDB |
30 variants for A2AI05
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388536284 | 77 | I>M | No | EVA | |
| rs3388530147 | 79 | R>P | No | EVA | |
| rs3388535484 | 80 | K>M | No | EVA | |
| rs3388532588 | 90 | M>I | No | EVA | |
| rs3388532974 | 118 | Q>H | No | EVA | |
| rs3388534386 | 128 | C>W | No | EVA | |
| rs28257621 | 143 | D>N | No | EVA | |
| rs3391322530 | 158 | P>S | No | EVA | |
| rs3388536317 | 196 | S>C | No | EVA | |
| rs1132260662 | 197 | S>* | No | EVA | |
| rs3388532581 | 202 | P>L | No | EVA | |
| rs3388531495 | 203 | P>S | No | EVA | |
| rs3388530139 | 210 | L>M | No | EVA | |
| rs3388533672 | 211 | A>T | No | EVA | |
| rs3388531453 | 214 | I>T | No | EVA | |
| rs3388533800 | 225 | F>I | No | EVA | |
| rs3391364179 | 241 | S>W | No | EVA | |
| rs230282300 | 278 | P>S | No | EVA | |
| rs216559205 | 325 | L>M | No | EVA | |
| rs28257626 | 347 | S>N | No | EVA | |
| rs3388535423 | 362 | H>Y | No | EVA | |
| rs3388535400 | 448 | K>I | No | EVA | |
| rs3388531447 | 475 | A>D | No | EVA | |
| rs3388535464 | 498 | T>S | No | EVA | |
| rs3388529482 | 500 | W>* | No | EVA | |
| rs13472087 | 518 | E>D | No | EVA | |
| rs3391292349 | 521 | Q>H | No | EVA | |
| rs28257633 | 543 | Q>H | No | EVA | |
| rs3388533114 | 545 | A>G | No | EVA | |
| rs3388533817 | 584 | A>V | No | EVA |
No associated diseases with A2AI05
14 regional properties for A2AI05
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Flavodoxin-like | 7 - 20 | IPR001094-1 |
| domain | Flavodoxin-like | 55 - 66 | IPR001094-2 |
| domain | Flavodoxin-like | 89 - 99 | IPR001094-3 |
| domain | Flavodoxin-like | 113 - 132 | IPR001094-4 |
| domain | Oxidoreductase FAD/NAD(P)-binding | 456 - 552 | IPR001433 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 242 - 252 | IPR001709-1 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 382 - 389 | IPR001709-2 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 416 - 425 | IPR001709-3 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 455 - 474 | IPR001709-4 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 479 - 488 | IPR001709-5 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 522 - 538 | IPR001709-6 |
| domain | Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding | 204 - 421 | IPR003097 |
| domain | Flavodoxin/nitric oxide synthase | 6 - 150 | IPR008254 |
| domain | FAD-binding domain, ferredoxin reductase-type | 206 - 448 | IPR017927 |
5 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. |
| intermediate filament cytoskeleton | Cytoskeletal structure made from intermediate filaments, typically organized in the cytosol as an extended system that stretches from the nuclear envelope to the plasma membrane. Some intermediate filaments run parallel to the cell surface, while others traverse the cytosol; together they form an internal framework that helps support the shape and resilience of the cell. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
| perinuclear region of cytoplasm | Cytoplasm situated near, or occurring around, the nucleus. |
10 GO annotations of molecular function
| Name | Definition |
|---|---|
| electron transfer activity | Any molecular entity that serves as an electron acceptor and electron donor in an electron transport chain. An electron transport chain is a process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient. |
| 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. |
| 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 binding | Binding to the reduced form, NADPH, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions. |
| 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. |
| oxidoreductase activity, acting on iron-sulfur proteins as donors, NAD or NADP as acceptor | Catalysis of an oxidation-reduction (redox) reaction in which an iron-sulfur protein acts as a hydrogen or electron donor and reduces NAD or NADP. |
| oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor | Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces a heme protein. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| cell death | Any biological process that results in permanent cessation of all vital functions of a cell. A cell should be considered dead when any one of the following molecular or morphological criteria is met: (1) the cell has lost the integrity of its plasma membrane; (2) the cell, including its nucleus, has undergone complete fragmentation into discrete bodies (frequently referred to as apoptotic bodies). The cell corpse (or its fragments) may be engulfed by an adjacent cell in vivo, but engulfment of whole cells should not be considered a strict criteria to define cell death as, under some circumstances, live engulfed cells can be released from phagosomes (see PMID:18045538). |
| cellular response to menadione | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a menadione stimulus. Menadione (also called vitamin K3) is a naphthoquinone having a methyl substituent at the 2-position. |
| electron transport chain | A process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors. |
| iron-sulfur cluster assembly | The incorporation of iron and exogenous sulfur into a metallo-sulfur cluster. |
6 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q1JPJ0 | NDOR1 | NADPH-dependent diflavin oxidoreductase 1 | Bos taurus (Bovine) | PR |
| Q9UBK8 | MTRR | Methionine synthase reductase | Homo sapiens (Human) | PR |
| Q9UHB4 | NDOR1 | NADPH-dependent diflavin oxidoreductase 1 | Homo sapiens (Human) | PR |
| Q8C1A3 | Mtrr | Methionine synthase reductase | Mus musculus (Mouse) | PR |
| P70313 | Nos3 | Nitric oxide synthase 3 | Mus musculus (Mouse) | SS |
| Q498R1 | Mtrr | Methionine synthase reductase | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MQVPQLLVLF | GSQTGTAQDE | AERLGREARR | RRLGCRVQAL | DSYSVANLIR | EPLVIFVCAT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TGQGDPPDNM | KNFWRFIFRK | SLPSSSLCQM | DFAVLGLGDS | SYAKFNFVAK | KLHRRLLQLG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GSALLPPCLG | DDQHELGPDA | AIDPWVGDLW | EKIMVMYPVP | LDIPEIPHGV | PLPSKFIFQF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LQEVPSIGAE | ELNIASSAPQ | TPPSELQPFL | APVITNQRVT | GPQHFQDVRL | IEFDITDSNI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SFAAGDVVFI | LPSNSEAHTQ | QFCQVLCLDP | NQFFTLKPRE | PGVPDPPGLP | QPCTVWNLVS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QYLDIASVPR | RSFFELLACL | SQHALEREKL | LELSSARGQE | ELWEYCSRPR | RTILEVLCDF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PHTAGAIPPD | YLLDLIPRIR | PRAFSIASSL | LAHPRRLQIL | VAVVKYQTRL | KEPRHGLCSS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| WLASLNPGQA | GPVRVPLWVR | PGSLVFPKTP | DTPIIMVGAG | TGVAPFRAAI | QERVAHGQTG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NFLFFGCRQR | DQDFYWQTEW | QKLEQKGWLT | LVTAFSREQE | QKVYVQHRLR | ELGPLVWELL |
| 550 | 560 | 570 | 580 | 590 | |
| DGQGAYFYLA | GNAKYLPTDV | SEALMSIFQE | EGRLSTADAS | AYLARLQQTL | RFQTETWA |