Q8C1A3
PR
Gene name |
Mtrr |
Protein name |
Methionine synthase reductase |
Names |
MSR, Aquacobalamin reductase, AqCbl reductase |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:210009 |
EC number |
1.16.1.8: With NAD(+) or NADP(+) 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 Q8C1A3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8C1A3-F1 | Predicted | AlphaFoldDB |
No variants for Q8C1A3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8C1A3 | |||||
No associated diseases with Q8C1A3
16 regional properties for Q8C1A3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Flavodoxin-like | 5 - 18 | IPR001094-1 |
| domain | Flavodoxin-like | 54 - 65 | IPR001094-2 |
| domain | Flavodoxin-like | 88 - 98 | IPR001094-3 |
| domain | Flavodoxin-like | 112 - 131 | IPR001094-4 |
| domain | Oxidoreductase FAD/NAD(P)-binding | 540 - 659 | IPR001433 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 305 - 315 | IPR001709-1 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 449 - 456 | IPR001709-2 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 485 - 494 | IPR001709-3 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 539 - 558 | IPR001709-4 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 570 - 579 | IPR001709-5 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 583 - 594 | IPR001709-6 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 620 - 636 | IPR001709-7 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 644 - 652 | IPR001709-8 |
| domain | Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding | 271 - 490 | IPR003097 |
| domain | Flavodoxin/nitric oxide synthase | 4 - 147 | IPR008254 |
| domain | FAD-binding domain, ferredoxin reductase-type | 269 - 531 | IPR017927 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.16.1.8 | With NAD(+) or NADP(+) as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 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. |
| 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. |
8 GO annotations of molecular function
| Name | Definition |
|---|---|
| [methionine synthase] reductase activity | Catalysis of the reaction: -cob(II)alamin + NADPH + H+ + S-adenosyl methionine = -methylcob(I)alamin + S-adenosylhomocysteine + NADP+. |
| 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. |
| 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 metal ions, NAD or NADP as acceptor | Catalysis of an oxidation-reduction in which the metal ion is reduced and NAD+ or NADP+ acts as an electron acceptor. |
9 GO annotations of biological process
| Name | Definition |
|---|---|
| cobalamin metabolic process | The chemical reactions and pathways involving cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom. |
| DNA methylation | The covalent transfer of a methyl group to either N-6 of adenine or C-5 or N-4 of cytosine. |
| folic acid metabolic process | The chemical reactions and pathways involving folic acid, pteroylglutamic acid. Folic acid is widely distributed as a member of the vitamin B complex and is essential for the synthesis of purine and pyrimidines. |
| homocysteine catabolic process | The chemical reactions and pathways resulting in the breakdown of homocysteine, the amino acid alpha-amino-gamma-mercaptobutanoic acid. |
| homocysteine metabolic process | The chemical reactions and pathways involving homocysteine, the amino acid alpha-amino-gamma-mercaptobutanoic acid. Homocysteine is an important intermediate in the metabolic reactions of its S-methyl derivative, methionine. |
| methionine biosynthetic process | The chemical reactions and pathways resulting in the formation of methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins. |
| negative regulation of cystathionine beta-synthase activity | Any process that stops, prevents or reduces the frequency, rate or extent of cystathionine beta-synthase activity. |
| protein stabilization | Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation. |
| S-adenosylmethionine cycle | A cyclic series of interconversions involving S-adenosylmethionine, S-adenosyl-L-homocysteine, L-cysteine, and L-methionine. Couples utilization of the methyl group of SAM with recycling of the homocysteinyl group and regeneration of methionine. |
11 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P29473 | NOS3 | Nitric oxide synthase, endothelial | Bos taurus (Bovine) | EV |
| P29474 | NOS3 | Nitric oxide synthase, endothelial | Homo sapiens (Human) | SS |
| P29475 | NOS1 | Nitric oxide synthase, brain | Homo sapiens (Human) | SS |
| Q9UBK8 | MTRR | Methionine synthase reductase | Homo sapiens (Human) | PR |
| A2AI05 | Ndor1 | NADPH-dependent diflavin oxidoreductase 1 | Mus musculus (Mouse) | PR |
| P70313 | Nos3 | Nitric oxide synthase 3 | Mus musculus (Mouse) | SS |
| Q28969 | NOS3 | Nitric oxide synthase 3 | Sus scrofa (Pig) | SS |
| Q62600 | Nos3 | Nitric oxide synthase 3 | Rattus norvegicus (Rat) | SS |
| P29476 | Nos1 | Nitric oxide synthase, brain | Rattus norvegicus (Rat) | SS |
| Q498R1 | Mtrr | Methionine synthase reductase | Rattus norvegicus (Rat) | PR |
| Q9FKW6 | LFNR1 | Ferredoxin--NADP reductase, leaf isozyme 1, chloroplastic | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRRFLLLYAT | QRGQAKAIAE | EISEQAVSHG | FSADLHCISE | SEKYDLKTET | GPLVMVVSTT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GTGDPPDTAR | KFVKEIHNKT | LPTDYFAHLR | YGLLGLGDSE | YTYFCNGGKV | IDKRLQELGA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QRFYDTGHAD | DCVGLELVVE | PWIDGLWAAL | TKHFKSLGGQ | ENMSDTLSRA | SDAPLSTAMK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PELLHIQSQV | ELLRLEDVGE | RDSELREQNE | TNRGQQGRIE | DFDSSLVHSV | PPLSQSSLSI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PAVPPEYLEV | HLQESLGQEE | NQASVPSGDP | SFQVPISKAI | RLTTNDAVKS | TLLLELDISK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IEFSHQPGDS | FNVTCPNSDR | EVEELLQRLQ | LADKRAHRVI | LKIKTDTKKK | GAALPAHVPE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GRSLQFILTW | CLEIRAVPKK | AFLRALAEHT | SSATEKRRLQ | ELCSKQGAAD | YNRFIRDASV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| CLLDLLLTFP | SCQPPLSLLL | EHLPKLQPRP | YSCASSSLRH | PDKLHFVFNI | VEFPPSTTAA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SPRKGVCTGW | LATLVAPFLQ | PNTDVSNADS | GDTLAPEIRI | SPRATNAFHL | PEDPSAPIIM |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VGPGTGVAPF | VGFLQHREKL | QEQHPDGKFG | AMWLFFGCRH | KDRDYLFREE | LRHFLKTGVL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| THLKVSFSRD | AAPDGEEAPA | KYVQDNLQRH | SQQVARTLLQ | ENGYIYVCGD | AKNMAKDVND |
| 670 | 680 | 690 | |||
| TLIGIISNEA | GVDKLEAMKT | LATLKQEKRY | LQDIWS |