EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.11.66 | gene kdmA or AN1060, phylogenetic analysis | Aspergillus nidulans |
1.14.11.69 | gene kdmA or AN1060, phylogenetic analysis | Aspergillus nidulans |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.11.66 | additional information | the kdmA mutant shows a significant increase in H3K36me3 during primary metabolism at the aflR and ipnA locus and some slightly higher levels at the aptA genes, the mutant has reduced levels of sterigmatocystin compared to wild-type, mutant phenotype, overview. Deletion of kdmA in Aspergillus nidulans produces both positive and negative changes in transcriptional readouts and the number of affected genes is different under different conditions. KdmA deletion alters expression pattern of secondary metabolism cluster genes in secondary metabolism phase, analysis of the heat map for mean expression of previously annotated secondary metabolism clusters. Deletion of kdmA causes light lethality and sensitivity to oxidative stress during vegetative growth | Aspergillus nidulans |
1.14.11.69 | additional information | the kdmA mutant shows a significant increase in H3K36me3 during primary metabolism at the aflR and ipnA locus and some slightly higher levels at the aptA genes, the mutant has reduced levels of sterigmatocystin compared to wild-type, mutant phenotype, overview. Deletion of kdmA in Aspergillus nidulans produces both positive and negative changes in transcriptional readouts and the number of affected genes is different under different conditions. KdmA deletion alters expression pattern of secondary metabolism cluster genes in secondary metabolism phase, analysis of the heat map for mean expression of previously annotated secondary metabolism clusters. Deletion of kdmA causes light lethality and sensitivity to oxidative stress during vegetative growth | Aspergillus nidulans |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.14.11.69 | nucleus | - |
Aspergillus nidulans | 5634 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.11.66 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2 | Aspergillus nidulans | - |
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2 | Aspergillus nidulans ATCC 38163 | - |
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2 | Aspergillus nidulans CBS 112.46 | - |
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2 | Aspergillus nidulans FGSC A4 | - |
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2 | Aspergillus nidulans M139 | - |
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2 | Aspergillus nidulans NRRL 194 | - |
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2 | Aspergillus nidulans | - |
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2 | Aspergillus nidulans ATCC 38163 | - |
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2 | Aspergillus nidulans CBS 112.46 | - |
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2 | Aspergillus nidulans FGSC A4 | - |
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2 | Aspergillus nidulans M139 | - |
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2 | Aspergillus nidulans NRRL 194 | - |
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.69 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2 | Aspergillus nidulans | - |
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.69 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2 | Aspergillus nidulans ATCC 38163 | - |
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.69 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2 | Aspergillus nidulans CBS 112.46 | - |
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.69 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2 | Aspergillus nidulans FGSC A4 | - |
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.69 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2 | Aspergillus nidulans M139 | - |
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.69 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2 | Aspergillus nidulans NRRL 194 | - |
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.69 | [histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2 | Aspergillus nidulans | - |
[histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.11.66 | Aspergillus nidulans | Q5BEH0 | i.e. Aspergillus nidulans | - |
1.14.11.66 | Aspergillus nidulans ATCC 38163 | Q5BEH0 | i.e. Aspergillus nidulans | - |
1.14.11.66 | Aspergillus nidulans CBS 112.46 | Q5BEH0 | i.e. Aspergillus nidulans | - |
1.14.11.66 | Aspergillus nidulans FGSC A4 | Q5BEH0 | i.e. Aspergillus nidulans | - |
1.14.11.66 | Aspergillus nidulans M139 | Q5BEH0 | i.e. Aspergillus nidulans | - |
1.14.11.66 | Aspergillus nidulans NRRL 194 | Q5BEH0 | i.e. Aspergillus nidulans | - |
1.14.11.69 | Aspergillus nidulans | Q5BEH0 | i.e. Aspergillus nidulans | - |
1.14.11.69 | Aspergillus nidulans ATCC 38163 | Q5BEH0 | i.e. Aspergillus nidulans | - |
1.14.11.69 | Aspergillus nidulans CBS 112.46 | Q5BEH0 | i.e. Aspergillus nidulans | - |
1.14.11.69 | Aspergillus nidulans FGSC A4 | Q5BEH0 | i.e. Aspergillus nidulans | - |
1.14.11.69 | Aspergillus nidulans M139 | Q5BEH0 | i.e. Aspergillus nidulans | - |
1.14.11.69 | Aspergillus nidulans NRRL 194 | Q5BEH0 | i.e. Aspergillus nidulans | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.11.66 | additional information | the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates | Aspergillus nidulans | ? | - |
? | |
1.14.11.66 | additional information | the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates | Aspergillus nidulans ATCC 38163 | ? | - |
? | |
1.14.11.66 | additional information | the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates | Aspergillus nidulans CBS 112.46 | ? | - |
? | |
1.14.11.66 | additional information | the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates | Aspergillus nidulans FGSC A4 | ? | - |
? | |
1.14.11.66 | additional information | the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates | Aspergillus nidulans M139 | ? | - |
? | |
1.14.11.66 | additional information | the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates | Aspergillus nidulans NRRL 194 | ? | - |
? | |
1.14.11.66 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans | [histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans ATCC 38163 | [histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans CBS 112.46 | [histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans FGSC A4 | [histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans M139 | [histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans NRRL 194 | [histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans | [histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans ATCC 38163 | [histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans CBS 112.46 | [histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans FGSC A4 | [histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans M139 | [histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.66 | [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans NRRL 194 | [histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.69 | additional information | the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates | Aspergillus nidulans | ? | - |
? | |
1.14.11.69 | additional information | the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates | Aspergillus nidulans ATCC 38163 | ? | - |
? | |
1.14.11.69 | additional information | the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates | Aspergillus nidulans CBS 112.46 | ? | - |
? | |
1.14.11.69 | additional information | the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates | Aspergillus nidulans FGSC A4 | ? | - |
? | |
1.14.11.69 | additional information | the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates | Aspergillus nidulans M139 | ? | - |
? | |
1.14.11.69 | additional information | the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates | Aspergillus nidulans NRRL 194 | ? | - |
? | |
1.14.11.69 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans | [histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.69 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans ATCC 38163 | [histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.69 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans CBS 112.46 | [histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.69 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans FGSC A4 | [histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.69 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans M139 | [histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.69 | [histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans NRRL 194 | [histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2 | - |
? | |
1.14.11.69 | [histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2 | - |
Aspergillus nidulans | [histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.11.66 | AN1060 | - |
Aspergillus nidulans |
1.14.11.66 | KdmA | - |
Aspergillus nidulans |
1.14.11.66 | More | see also EC 1.14.11.69 | Aspergillus nidulans |
1.14.11.69 | AN1060 | - |
Aspergillus nidulans |
1.14.11.69 | KDM | - |
Aspergillus nidulans |
1.14.11.69 | KdmA | - |
Aspergillus nidulans |
1.14.11.69 | More | see also EC 1.14.11.66 | Aspergillus nidulans |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.14.11.66 | evolution | the enzyme encoded by gene AN1060 (designated as kdmA) is a member of the mammalian KDM4 family of proteins (also known as JHDM3/JMJD2 in mammals) | Aspergillus nidulans |
1.14.11.66 | malfunction | the kdmA mutant shows a significant increase in H3K36me3 during primary metabolism at the aflR and ipnA locus and some slightly higher levels at the aptA genes, the mutant has reduced levels of sterigmatocystin compared to wild-type. Manipulation of kdmA expression reveals genetic and environmental interactions including lethality under light. Deletion of kdmA causes light lethality and sensitivity to oxidative stress during vegetative growth to chronic oxidative stress | Aspergillus nidulans |
1.14.11.66 | physiological function | KdmA, a histone H3 demethylase with bipartite function, differentially regulates primary and secondary metabolism in Aspergillus nidulans. KdmA displays locus-specific histone H3 lysine demethylation activity | Aspergillus nidulans |
1.14.11.69 | evolution | the enzyme encoded by gene AN1060 (designated as kdmA) is a member of the mammalian KDM4 family of proteins (also known as JHDM3/JMJD2 in mammals) | Aspergillus nidulans |
1.14.11.69 | malfunction | the kdmA mutant shows a significant increase in H3K36me3 during primary metabolism at the aflR and ipnA locus and some slightly higher levels at the aptA genes, the mutant has reduced levels of sterigmatocystin compared to wild-type. Manipulation of kdmA expression reveals genetic and environmental interactions including lethality under light. Deletion of kdmA causes light lethality and sensitivity to oxidative stress during vegetative growth to chronic oxidative stress | Aspergillus nidulans |
1.14.11.69 | physiological function | KdmA, a histone H3 demethylase with bipartite function, differentially regulates primary and secondary metabolism in Aspergillus nidulans. KdmA displays locus-specific histone H3 lysine demethylation activity | Aspergillus nidulans |