EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.283 | gene CANTEDRAFT_112488 | Yamadazyma tenuis |
1.1.1.283 | gene GRE2 | Saccharomyces cerevisiae |
1.1.1.283 | gene GRE3 | Saccharomyces cerevisiae |
1.1.1.283 | gene GRP2 | Yarrowia lipolytica |
1.1.1.283 | gene PAS_chr3_0744 | Komagataella phaffii |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.1.1.283 | cytosol | - |
[Candida] boidinii | 5829 | - |
1.1.1.283 | cytosol | - |
Lipomyces starkeyi | 5829 | - |
1.1.1.283 | cytosol | - |
Candida tropicalis | 5829 | - |
1.1.1.283 | cytosol | - |
Wickerhamomyces anomalus | 5829 | - |
1.1.1.283 | cytosol | - |
Kluyveromyces lactis | 5829 | - |
1.1.1.283 | cytosol | - |
Blastobotrys adeninivorans | 5829 | - |
1.1.1.283 | cytosol | - |
[Candida] arabinofermentans | 5829 | - |
1.1.1.283 | cytosol | - |
Saccharomyces cerevisiae | 5829 | - |
1.1.1.283 | cytosol | - |
Komagataella phaffii | 5829 | - |
1.1.1.283 | cytosol | - |
Yamadazyma tenuis | 5829 | - |
1.1.1.283 | cytosol | - |
Yarrowia lipolytica | 5829 | - |
1.1.1.283 | cytosol | - |
Candida sojae | 5829 | - |
1.1.1.283 | cytosol | - |
Suhomyces tanzawaensis | 5829 | - |
1.1.1.283 | cytosol | - |
Kazachstania africana | 5829 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.283 | methylglyoxal + NADPH + H+ | [Candida] boidinii | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Lipomyces starkeyi | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Candida tropicalis | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Wickerhamomyces anomalus | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Kluyveromyces lactis | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Blastobotrys adeninivorans | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | [Candida] arabinofermentans | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Saccharomyces cerevisiae | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Komagataella phaffii | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Yamadazyma tenuis | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Yarrowia lipolytica | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Candida sojae | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Suhomyces tanzawaensis | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Kazachstania africana | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Yamadazyma tenuis VKM Y-70 | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Yamadazyma tenuis BCRC 21748 | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Yamadazyma tenuis CBS 615 | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Komagataella phaffii ATCC 20864 | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Saccharomyces cerevisiae ATCC 204508 | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Yamadazyma tenuis NBRC 10315 | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Yamadazyma tenuis ATCC 10573 | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Komagataella phaffii GS115 | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Yamadazyma tenuis JCM 9827 | - |
(S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | Yamadazyma tenuis NRRL Y-1498 | - |
(S)-lactaldehyde + NADP+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.283 | Blastobotrys adeninivorans | - |
Arxula adeninivorans | - |
1.1.1.283 | Candida sojae | - |
- |
- |
1.1.1.283 | Candida tropicalis | - |
- |
- |
1.1.1.283 | Kazachstania africana | - |
- |
- |
1.1.1.283 | Kluyveromyces lactis | - |
- |
- |
1.1.1.283 | Komagataella phaffii | C4R5F8 | Pichia pastoris | - |
1.1.1.283 | Komagataella phaffii ATCC 20864 | C4R5F8 | Pichia pastoris | - |
1.1.1.283 | Komagataella phaffii GS115 | C4R5F8 | Pichia pastoris | - |
1.1.1.283 | Lipomyces starkeyi | - |
- |
- |
1.1.1.283 | no activity in Dekkera bruxellensis | - |
- |
- |
1.1.1.283 | no activity in Schizosaccharomyces pombe | - |
- |
- |
1.1.1.283 | Saccharomyces cerevisiae | P38715 | - |
- |
1.1.1.283 | Saccharomyces cerevisiae | Q12068 | - |
- |
1.1.1.283 | Saccharomyces cerevisiae ATCC 204508 | P38715 | - |
- |
1.1.1.283 | Saccharomyces cerevisiae ATCC 204508 | Q12068 | - |
- |
1.1.1.283 | Suhomyces tanzawaensis | - |
- |
- |
1.1.1.283 | Wickerhamomyces anomalus | - |
- |
- |
1.1.1.283 | Yamadazyma tenuis | G3AZL9 | Yamadazyma tenuis | - |
1.1.1.283 | Yamadazyma tenuis ATCC 10573 | G3AZL9 | Yamadazyma tenuis | - |
1.1.1.283 | Yamadazyma tenuis BCRC 21748 | G3AZL9 | Yamadazyma tenuis | - |
1.1.1.283 | Yamadazyma tenuis CBS 615 | G3AZL9 | Yamadazyma tenuis | - |
1.1.1.283 | Yamadazyma tenuis JCM 9827 | G3AZL9 | Yamadazyma tenuis | - |
1.1.1.283 | Yamadazyma tenuis NBRC 10315 | G3AZL9 | Yamadazyma tenuis | - |
1.1.1.283 | Yamadazyma tenuis NRRL Y-1498 | G3AZL9 | Yamadazyma tenuis | - |
1.1.1.283 | Yamadazyma tenuis VKM Y-70 | G3AZL9 | Yamadazyma tenuis | - |
1.1.1.283 | Yarrowia lipolytica | A0A1D8NEA1 | Candida lipolytica | - |
1.1.1.283 | [Candida] arabinofermentans | - |
- |
- |
1.1.1.283 | [Candida] boidinii | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
[Candida] boidinii | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Lipomyces starkeyi | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Candida tropicalis | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Wickerhamomyces anomalus | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Kluyveromyces lactis | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Blastobotrys adeninivorans | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
[Candida] arabinofermentans | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Saccharomyces cerevisiae | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Komagataella phaffii | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Yamadazyma tenuis | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Yarrowia lipolytica | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Candida sojae | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Suhomyces tanzawaensis | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Kazachstania africana | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Yamadazyma tenuis VKM Y-70 | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Yamadazyma tenuis BCRC 21748 | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Yamadazyma tenuis CBS 615 | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Komagataella phaffii ATCC 20864 | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Saccharomyces cerevisiae ATCC 204508 | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Yamadazyma tenuis NBRC 10315 | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Yamadazyma tenuis ATCC 10573 | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Komagataella phaffii GS115 | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Yamadazyma tenuis JCM 9827 | (S)-lactaldehyde + NADP+ | - |
? | |
1.1.1.283 | methylglyoxal + NADPH + H+ | - |
Yamadazyma tenuis NRRL Y-1498 | (S)-lactaldehyde + NADP+ | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.283 | CANTEDRAFT_112488 | - |
Yamadazyma tenuis |
1.1.1.283 | Gre2 | - |
Yamadazyma tenuis |
1.1.1.283 | Gre2 | - |
Saccharomyces cerevisiae |
1.1.1.283 | GRE3 | - |
Saccharomyces cerevisiae |
1.1.1.283 | GRP2 | - |
Yarrowia lipolytica |
1.1.1.283 | methylglyoxal reductase | - |
[Candida] boidinii |
1.1.1.283 | methylglyoxal reductase | - |
Lipomyces starkeyi |
1.1.1.283 | methylglyoxal reductase | - |
Candida tropicalis |
1.1.1.283 | methylglyoxal reductase | - |
Wickerhamomyces anomalus |
1.1.1.283 | methylglyoxal reductase | - |
Kluyveromyces lactis |
1.1.1.283 | methylglyoxal reductase | - |
Blastobotrys adeninivorans |
1.1.1.283 | methylglyoxal reductase | - |
[Candida] arabinofermentans |
1.1.1.283 | methylglyoxal reductase | - |
Saccharomyces cerevisiae |
1.1.1.283 | methylglyoxal reductase | - |
Komagataella phaffii |
1.1.1.283 | methylglyoxal reductase | - |
Yamadazyma tenuis |
1.1.1.283 | methylglyoxal reductase | - |
Yarrowia lipolytica |
1.1.1.283 | methylglyoxal reductase | - |
Candida sojae |
1.1.1.283 | methylglyoxal reductase | - |
Suhomyces tanzawaensis |
1.1.1.283 | methylglyoxal reductase | - |
Kazachstania africana |
1.1.1.283 | MGR | - |
[Candida] boidinii |
1.1.1.283 | MGR | - |
Lipomyces starkeyi |
1.1.1.283 | MGR | - |
Candida tropicalis |
1.1.1.283 | MGR | - |
Wickerhamomyces anomalus |
1.1.1.283 | MGR | - |
Kluyveromyces lactis |
1.1.1.283 | MGR | - |
Blastobotrys adeninivorans |
1.1.1.283 | MGR | - |
[Candida] arabinofermentans |
1.1.1.283 | MGR | - |
Saccharomyces cerevisiae |
1.1.1.283 | MGR | - |
Komagataella phaffii |
1.1.1.283 | MGR | - |
Yamadazyma tenuis |
1.1.1.283 | MGR | - |
Yarrowia lipolytica |
1.1.1.283 | MGR | - |
Candida sojae |
1.1.1.283 | MGR | - |
Suhomyces tanzawaensis |
1.1.1.283 | MGR | - |
Kazachstania africana |
1.1.1.283 | PAS_chr3_0744 | - |
Komagataella phaffii |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.283 | NADPH | - |
[Candida] boidinii | |
1.1.1.283 | NADPH | - |
Lipomyces starkeyi | |
1.1.1.283 | NADPH | - |
Candida tropicalis | |
1.1.1.283 | NADPH | - |
Wickerhamomyces anomalus | |
1.1.1.283 | NADPH | - |
Kluyveromyces lactis | |
1.1.1.283 | NADPH | - |
Blastobotrys adeninivorans | |
1.1.1.283 | NADPH | - |
[Candida] arabinofermentans | |
1.1.1.283 | NADPH | - |
Saccharomyces cerevisiae | |
1.1.1.283 | NADPH | - |
Komagataella phaffii | |
1.1.1.283 | NADPH | - |
Yamadazyma tenuis | |
1.1.1.283 | NADPH | - |
Yarrowia lipolytica | |
1.1.1.283 | NADPH | - |
Candida sojae | |
1.1.1.283 | NADPH | - |
Suhomyces tanzawaensis | |
1.1.1.283 | NADPH | - |
Kazachstania africana |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.1.1.283 | evolution | the organism contains 1 MGR gene copy | Lipomyces starkeyi |
1.1.1.283 | evolution | the organism contains 2 MGR gene copies | Kluyveromyces lactis |
1.1.1.283 | evolution | the organism contains 2 MGR gene copies | Yamadazyma tenuis |
1.1.1.283 | evolution | the organism contains 3 MGR gene copies | Candida sojae |
1.1.1.283 | evolution | the organism contains 3 MGR gene copies | Kazachstania africana |
1.1.1.283 | evolution | the organism contains 4 MGR gene copies | Blastobotrys adeninivorans |
1.1.1.283 | evolution | the organism contains 4 MGR gene copies | [Candida] arabinofermentans |
1.1.1.283 | evolution | the organism contains 4 MGR gene copies | Saccharomyces cerevisiae |
1.1.1.283 | evolution | the organism contains 5 MGR gene copies | [Candida] boidinii |
1.1.1.283 | evolution | the organism contains 6 MGR gene copies | Komagataella phaffii |
1.1.1.283 | evolution | the organism contains 7 MGR gene copies | Suhomyces tanzawaensis |
1.1.1.283 | evolution | the organism contains 8 MGR gene copies | Wickerhamomyces anomalus |
1.1.1.283 | evolution | the organism contains 9 MGR gene copies | Yarrowia lipolytica |
1.1.1.283 | evolution | the organism contains diverse MGR gene copies | Candida tropicalis |
1.1.1.283 | metabolism | metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview | [Candida] boidinii |
1.1.1.283 | metabolism | metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview | Lipomyces starkeyi |
1.1.1.283 | metabolism | metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview | Candida tropicalis |
1.1.1.283 | metabolism | metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview | Wickerhamomyces anomalus |
1.1.1.283 | metabolism | metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview | Kluyveromyces lactis |
1.1.1.283 | metabolism | metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview | Blastobotrys adeninivorans |
1.1.1.283 | metabolism | metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview | [Candida] arabinofermentans |
1.1.1.283 | metabolism | metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview | Saccharomyces cerevisiae |
1.1.1.283 | metabolism | metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview | Komagataella phaffii |
1.1.1.283 | metabolism | metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview | Yamadazyma tenuis |
1.1.1.283 | metabolism | metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview | Yarrowia lipolytica |
1.1.1.283 | metabolism | metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview | Candida sojae |
1.1.1.283 | metabolism | metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview | Suhomyces tanzawaensis |
1.1.1.283 | metabolism | metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview | Kazachstania africana |
1.1.1.283 | additional information | evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance | [Candida] boidinii |
1.1.1.283 | additional information | evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance | Lipomyces starkeyi |
1.1.1.283 | additional information | evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance | Candida tropicalis |
1.1.1.283 | additional information | evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance | Wickerhamomyces anomalus |
1.1.1.283 | additional information | evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance | Kluyveromyces lactis |
1.1.1.283 | additional information | evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance | Blastobotrys adeninivorans |
1.1.1.283 | additional information | evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance | [Candida] arabinofermentans |
1.1.1.283 | additional information | evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance | Saccharomyces cerevisiae |
1.1.1.283 | additional information | evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance | Komagataella phaffii |
1.1.1.283 | additional information | evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance | Yamadazyma tenuis |
1.1.1.283 | additional information | evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance | Yarrowia lipolytica |
1.1.1.283 | additional information | evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance | Candida sojae |
1.1.1.283 | additional information | evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance | Suhomyces tanzawaensis |
1.1.1.283 | additional information | evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance | Kazachstania africana |
1.1.1.283 | physiological function | model for MGR role in oxidative imbalance, overview | [Candida] boidinii |
1.1.1.283 | physiological function | model for MGR role in oxidative imbalance, overview | Lipomyces starkeyi |
1.1.1.283 | physiological function | model for MGR role in oxidative imbalance, overview | Candida tropicalis |
1.1.1.283 | physiological function | model for MGR role in oxidative imbalance, overview | Wickerhamomyces anomalus |
1.1.1.283 | physiological function | model for MGR role in oxidative imbalance, overview | Kluyveromyces lactis |
1.1.1.283 | physiological function | model for MGR role in oxidative imbalance, overview | Blastobotrys adeninivorans |
1.1.1.283 | physiological function | model for MGR role in oxidative imbalance, overview | [Candida] arabinofermentans |
1.1.1.283 | physiological function | model for MGR role in oxidative imbalance, overview | Saccharomyces cerevisiae |
1.1.1.283 | physiological function | model for MGR role in oxidative imbalance, overview | Komagataella phaffii |
1.1.1.283 | physiological function | model for MGR role in oxidative imbalance, overview | Yamadazyma tenuis |
1.1.1.283 | physiological function | model for MGR role in oxidative imbalance, overview | Yarrowia lipolytica |
1.1.1.283 | physiological function | model for MGR role in oxidative imbalance, overview | Candida sojae |
1.1.1.283 | physiological function | model for MGR role in oxidative imbalance, overview | Suhomyces tanzawaensis |
1.1.1.283 | physiological function | model for MGR role in oxidative imbalance, overview | Kazachstania africana |