FOG04504
EOG8SF7N6
EOG8WH722
sce:absent
Genes: 10
AspGD DescriptionOrtholog(s) have role in conidiophore development, oxidation-reduction process and intracellular localization|Has domain(s) with predicted choline dehydrogenase activity, flavin adenine dinucleotide binding, oxidoreductase activity, acting on CH-OH group of donors activity and role in alcohol metabolic process, oxidation-reduction process|Ortholog(s) have role in conidiophore development, oxidation-reduction process and intracellular localization
References
Hortschansky P, et al. (2007 Jul 11). Interaction of HapX with the CCAAT-binding complex--a novel mechanism of gene regulation by iron.
Levasseur A, et al. (2008 May). FOLy: an integrated database for the classification and functional annotation of fungal oxidoreductases potentially involved in the degradation of lignin and related aromatic compounds.
Shimizu M, et al. (2009 Jan). Proteomic analysis of Aspergillus nidulans cultured under hypoxic conditions.
Schinko T, et al. (2010 Nov). Transcriptome analysis of nitrate assimilation in Aspergillus nidulans reveals connections to nitric oxide metabolism.
Pusztahelyi T, et al. (2011 Feb). Comparison of transcriptional and translational changes caused by long-term menadione exposure in Aspergillus nidulans.
Etxebeste O, et al. (2012). GmcA is a putative glucose-methanol-choline oxidoreductase required for the induction of asexual development in Aspergillus nidulans.
FOG04505
EOG8SF7N6
sce:absent
Genes: 6
AspGD DescriptionOrtholog(s) have role in secondary metabolite biosynthetic process|Ortholog(s) have role in secondary metabolite biosynthetic process|Has domain(s) with predicted flavin adenine dinucleotide binding, oxidoreductase activity, acting on CH-OH group of donors activity and role in oxidation-reduction process|Has domain(s) with predicted choline dehydrogenase activity, flavin adenine dinucleotide binding, oxidoreductase activity, acting on CH-OH group of donors activity and role in alcohol metabolic process, oxidation-reduction process|Has domain(s) with predicted choline dehydrogenase activity, flavin adenine dinucleotide binding, oxidoreductase activity, acting on CH-OH group of donors activity and role in alcohol metabolic process, oxidation-reduction process|Has domain(s) with predicted choline dehydrogenase activity, flavin adenine dinucleotide binding, oxidoreductase activity, acting on CH-OH group of donors activity and role in alcohol metabolic process, oxidation-reduction process
References
Brown DW, et al. (1996 Feb 20). Twenty-five coregulated transcripts define a sterigmatocystin gene cluster in Aspergillus nidulans.
Fernandes M, et al. (1998 Jun). Sequence-specific binding by Aspergillus nidulans AflR, a C6 zinc cluster protein regulating mycotoxin biosynthesis.
Bok JW, et al. (2006 Jan). Genomic mining for Aspergillus natural products.
Levasseur A, et al. (2008 May). FOLy: an integrated database for the classification and functional annotation of fungal oxidoreductases potentially involved in the degradation of lignin and related aromatic compounds.
Sanchez JF, et al. (2012 Aug 1). Identification and molecular genetic analysis of the cichorine gene cluster in <i>Aspergillus nidulans.</i>
de Souza WR, et al. (2013). Identification of metabolic pathways influenced by the G-protein coupled receptors GprB and GprD in Aspergillus nidulans.
FOG04506
EOG8SF7N6
sce:absent
Genes: 4
AspGD DescriptionHas domain(s) with predicted flavin adenine dinucleotide binding, oxidoreductase activity, acting on CH-OH group of donors activity and role in oxidation-reduction process|Putative aryl-alcohol oxidase|Has domain(s) with predicted choline dehydrogenase activity, flavin adenine dinucleotide binding, oxidoreductase activity, acting on CH-OH group of donors activity and role in alcohol metabolic process, oxidation-reduction process
References
Shimizu M, et al. (2009 Jan). Proteomic analysis of Aspergillus nidulans cultured under hypoxic conditions.
Sato I, et al. (2009 Mar 20). The glutathione system of Aspergillus nidulans involves a fungus-specific glutathione S-transferase.