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Organism related
Word Map for Organism Aspergillus niger
- Aspergillus niger
- fumigatus
- esterase
- glucoamylase
- nidulans
- terreus
- xylanase
- versicolor
- phytase
- rhizopus
- aspergillosis
- mycotoxin
- mucor
- alternata
- endoglucanase
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ochratoxin
- cellulases
- aflatoxin
- reesei
- crassa
- chrysogenum
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aspergilli
- ochraceus
- carbonarius
- pastoris
- pectinase
- polygalacturonase
- beta-glucosidase
- viride
- aculeatus
- citrinum
- fumonisins
- itraconazole
- awamori
- lipases
- parasiticus
- voriconazole
- stolonifer
- bagasse
- endoxylanase
- lunata
- expansum
- notatum
- caspofungin
- alpha-galactosidase
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feruloylated
- endoprotease
- arabinoxylans
- verrucosum
- catalases
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bioleaching
TaxTree of Organism Aspergillus niger
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EC NUMBER 
COMMENTARY 
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preliminary BRENDA-supplied EC number
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-hydroxymandelate degradation
bile acid biosynthesis, neutral pathway
degradation of aromatic, nitrogen containing compounds
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ketogluconate metabolism
methylaspartate cycle
oxalate biosynthesis
resorcinol degradation
suberin monomers biosynthesis
urea cycle
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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285665, 712023, 285787, 668063, 389419, 389421, 286357, 684945, 286644, 655613, 286749, 286793, 740181, 760657, 287005, 287289, 287290, 207955, 761153, 760777, 722316, 721358, 723997, 389787, 389788, 389790, 389792, 389793, 389794, 389796, 389797, 389798, 389799, 389801, 389802, 389803, 389804, 389805, 389806, 389807, 389813, 389815, 389816, 389817, 389819, 389821, 389822, 389823, 389824, 389825, 389827, 389829, 389834, 389836, 389837, 654143, 654185, 654358, 654659, 654780, 654909, 655079, 655711, 656254, 656562, 656782, 657249, 675186, 677260, 695559, 695600, 695790, 696068, 696369, 696777, 696864, 696865, 698321, 699078, 699600, 699771, 699922, 699941, 700599, 723947, 724880, 724884, 725199, 725789, 726413, 741479, 742129, 743171, 743644, 742213, 743775, 672872, 696884, 710858, 710908, 712533, 712857, 713259, 348275, 740195, 288169, 349015, 390692, 391374, 697654, 686726, 741527, 743532, 675825, 394561, 743095, 743099, 701487, 705128, 391953, 686921, 654190, 658230, 658464, 658564, 658465, 657645, 659861,
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700255, 685428, 685429, 688784, 690105, 726565, 727055, 727205, 728045, 741835, 742144, 743105, 743277, 743283, 743744, 743857, 746771, 746773, 747341, 747343, 747675, 748768, 695717, 686060, 391951, 391953, 491169, 677293, 677627, 677744, 679050, 679061, 679840, 680967, 682613, 699073, 707241, 737333, 737802, 739566, 745143, 746067, 714497, 729418, 729456, 751703, 730728, 730886, 114251, 749503, 749519, 751164, 654519, 707832, 749631, 750226, 750231, 751980, 752083, 666820, 678084, 646670, 660943, 666369, 649347
Q9P8R5, P13006, P46882, Q12556, Q00078, O42807, Q8WZI8, P34752, P69328, Q8TG09, O74641, Q9P8F4, A1XP58, Q8TFP1, Q9UR30, Q96VT7, Q8J219
SwissProt
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696988, 710970, 761084, 741418, 761153, 741576, 743193, 743824, 742640, 744139, 743643, 741716, 735929, 757903, 758967, 641066, 671410, 671462, 737422, 751146, 751060, 752106, 671497, 751836, 692398, 749604, 750431, 681717, 744006, 735455, 749677, 750888, 751980, 709554, 729014, 751243, 744626, 751303, 696466, 135842, 749692, 750602, 708849, 750893, 749475, 744078, 713873, 739579, 752093, 750586, 750785, 750829, 750855, 716839, 713698, 288845, 288846, 742156, 750154, 750082, 754912, 753726, 666365, 709429, 753407, 752543, 719168, 712260, 718670, 734496, 687682, 722316, 693684, 747890, 749419, 702388, 649946, 747889
A2QAC0, G3XRE5, A0A1D8RK43, A8DRH9, Q0PGS3, Q9HFQ1, A2R4V5, G3XZT7, B6V7E4, P17549, G3Y419, T1SGS1, A2QH83, Q92407, P78985, U4MZ33, A0A345K402, G3YAL0, A2QIR3, A7YN26, A2QZI3, B3VPB3, G8GYH6, P34754, Q6T9Z6, O74705, O74706, A0A221C6S1, A5ABL2, Q8J229, F5CI28, I3QKR9, P55329, A0A0B4UL66, P26213, P26214, Q9P4W2, A0PCH8, A2QJF7, P56526, A0A075EKG1, B6HYI9, A0A023J5W7, R9W5L0, G5D7B5, D6QST5, P42254, A2QKT4, Q9UVS8, P87160, Q5EC68, Q96VT2, A2QR21, A2R3L3, W8R465, A9QXE0, A2R6M7, Q7Z986, A8DRH7, Q2L887, G3Y8T6, G3YE52, G3Y683, G3XPU3, A2QV36, Q9C2Z0, A2R3C7
UniProt
2 methylglyoxylate reductases: MGR I and MGR II, similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+
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a xerophilic strain isolated from the Mexican semi-desert
UniProt
Aspergillus niger responds to cell wall stress by transcriptional activation of cell wall reinforcing genes including agsA (encoding a alpha-1,3-glucan synthase) through an RIm1p-like transcription factor.
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ATCC 9142. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
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BCC18081 (TR170), the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
UniProt
bifunctional alpha-galactosidase and alpha-N-acetylgalactosaminidase
UniProt
bifunctional alpha-N-acetylgalactosaminidase and alpha-N-acetylgalactosidase
UniProt
bifunctional enzyme: quinate (shikimate) dehydrogenase, different from EC 1.1.1.25
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coexpression of enzyme with Trichoderma reesei xylanayse II in Saccharomyces cerevisiae
SwissProt
enzyme is induced in the presence of galactofuranoside containing glycoconjugates
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FS-44, 5'-PDase hyperproductive mutant: bifunctional enzyme: cyclic-ribonucleotide phosphomutase-5'-phosphodiesterase
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GDH from Aspergillus terreus is kinetically distinct from GDH of Aspergilli niger
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iron-chlorin protein also catalyzes methyl viologen-linked reduction of hydroxylamine and that of nitrite at a slower rate
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isolated from soil samples collected in Northeast Parana State in Brazil
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locally isolated Aspergillus niger, wild-type and deoxy-D-glucose-resistant mutant
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NRRL 3135. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
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strain 92 and strain NRRL 3135. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissPRot
strain MTCC 2425, and a strain isolated from a composite tannery effluent collected from a local tannery
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strain MYA 135, formerly strain 419, constitutive and inducible enzymes
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strain NRRL3135. The T213 phytase differs from NRRL 3135 phytase at 12 amino acid residues.S13 in NRRL 3135 and A14 in T213, S30 in NRRL 3135 and T14 in T213, E66 in NRRL 3135 and D66 in T213, D89 in NRRL 3135 and E89 in T213, A106 in NRRL 3135 and V106 in T213, V155 in NRRL 3135 and I155 in T213, K171 in NRRL 3135 and E171 in T213, V236 in NRRL 3135 and A236 in T213, N292 in NRRL 3135 and H292 in T213, Q297 in NRRL 3135 and R297 in T213, S345 in NRRL 3135 and N345 in T213, V438 in NRRL 3135 and I438 in T213. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
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strains CBS 513.88, NRRL3122, and N402, isozymes AgtA and AgtB encoded by genes agtA and agtB
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the CBS 141257 strain is obtained by transformation of strain N593.20 with uridine (pyrG) from Aspergillus oryzae
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The enzyme exhibits phytase and acid phosphatase activity. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
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The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
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The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
SwissProt
The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified. Growth and phosphorus nutrition of the plants supplied with phytate is improved significantly when the phytase gene from Aspergillus niger is introduced.The Aspergillus phytase is only effective when secreted as an extracellular enzyme by inclusion of the signal peptide sequence from the carrot extensin gene
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the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
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The T213 phytase differs from NRRL 3135 phytase at 12 amino acid residues.S13 in NRRL 3135 and A14 in T213, S30 in NRRL 3135 and T14 in T213, E66 in NRRL 3135 and D66 in T213, D89 in NRRL 3135 and E89 in T213, A106 in NRRL 3135 and V106 in T213, V155 in NRRL 3135 and I155 in T213, K171 in NRRL 3135 and E171 in T213, V236 in NRRL 3135 and A236 in T213, N292 in NRRL 3135 and H292 in T213, Q297 in NRRL 3135 and R297 in T213, S345 in NRRL 3135 and N345 in T213, V438 in NRRL 3135 and I438 in T213. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
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two amine oxidases isolated: the first one corresponds to the copper-dependent enzyme, the second one is an evolutionary prototype form of MAO-A and B
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van Teighem. The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
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wild-type strain NIAB 280, and its derivative the catabolite-derepressed mutant strain M125
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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endoxylanase production is optimized using agricultural bagasses and cost 20 times less than enzyme production using synthetic xylan
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389796, 389797, 389798, 389801, 389802, 389804, 389816, 389821, 389834, 389837, 677260, 723947, 724884, 725789, 726413, 741479, 685428, 685429, 688784, 690105, 741835, 742144, 743105, 743283, 723981, 650815, 750251, 693493, 714025, 716930, 664207, 665281, 680931, 729537, 717405, 744006, 717110, 749631, 752083, 709554, 750602, 136395, 750231, 208785, 208798, 657384
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commercial preparation of Koch-Light Ltd. Colnbrook, England
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industrial strain, Aspergillus niger/Talaromyces emersonii enzyme mixture containing Aspergillus niger acetylxylan esterase and Tlaromyces emersonii acetyl esterase
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proctase powder, crude enzyme powder from waters of Koji cultures
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Sumizyme AC, Shin-Nippon Chemical Industries Co., Ltd., cellulase activity 2-5 unit/mg
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740181, 668063, 722316, 741576, 389805, 672872, 695790, 696865, 742213, 348275, 675825, 391951, 391953, 438964, 438875, 438877, 440256, 741716, 487424, 488074, 729072, 640480, 671410, 641513, 640318, 651740, 134747, 677764, 208564, 208567, 326377, 668812, 752543, 712784, 684638, 209833, 4560, 4576, 747418, 24216, 3714
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highest activity found in rapidly growing mycelium, glucose-NH4+ or glucose-peptone medium
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solid-state fermentation in double-surface bioreactor, fermentation method optimization, overview
additional information
activity of wild-type and mutant M12 GOx during fermentation, overview
additional information
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culture conditions for enzyme production, overview
additional information
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culture conditions of wild-type and mutant strains: preferred as carbohydrate and nitrogen sources are wheat bran and corn steep liquor, pH 5.5-6.5, optimal conditions, overview, fermentation kinetics of wild-type and mutant strains with different substrates in submerged fermentations, overview
additional information
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cultures are grown on agar plates at pH 4.0 with the cutinase model substrate polycaprolactone as a carbon source
additional information
extracellular enzyme activity and L-DOPA production are maximal when glucose and peptone are employed as carbon source and nitrogen source, respectively, in the medium, and are enhanced notably when Cu2+ is supplemented
additional information
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from submerged or solid-state cultures with higher enzyme activity in the latter
additional information
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inductive synthesis of levoglucosan kinase, the organism grows well on levoglucosan as sole carbon source, fermenting it into citric acid with a yield comparable to that on glucose
additional information
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optimization of growth conditions, enzyme expression depends on carbon source for growth, glucose nearly completely suppresses enzyme expression, while wheat bran, rice bran, and cellulose induce it, the enzyme prefers monosaccharides to disaccharides for growth, overview
additional information
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optimization of production of beta-glucanase with barley flour as the sole carbon source
additional information
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poor expression of MpdA in conidiospores, expression anaylsis
additional information
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production of high levels of L-asparaginase in solid state fermentation, using agro-wastes from three leguminous crops (bran of Cajanus cajan, Phaseolus mungo, and Glycine max)
additional information
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the enzyme production is increased by 3.6fold with statistically optimized medium when compared to the basal medium, optimization, overview
additional information
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the highest enzyme production by both the strains is 3% (w/v) sucrose and 3% (w/v) peptone, or 3.5% (w/v) total sugars present in cane molasses and 1.5% (w/v) yeast powder
additional information
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up to 23% of the total FAE activity is found in detergent extracts of the residues of leaf tissue of plants transformed with FAEA targeted to the endoplasmic reticulum or Golgi, particularly those plants which show higher activity in soluble extracts such as plants T36 and T38. 50%60% of the FAEA activity is found in apoplast extracts
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
recombinant protein in expressed in Arabidopsis thaliana
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recombinant protein, localization to cell suface of Pichia pastoris with a glycosylphosphatidylinositiol anchoring system
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isoform EroA is retained in the ER lumen by a C-terminal retention motif
additional information
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12% of glucose oxidase activity in the stationary phase and 16% of glucose oxidase activity in the mid-exponential phase is localised in the cytoplasm
P13006, Q0PGS3, A0A140CTD1, A0A0G3ZA16, O42807, Q8WZI8, O93838, P34752, B3VPB3, A5ABL2, O74641, A2QJF7, P56526, P29853, G5D7B5, A1XP58, Q8J219
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742213, 741835, 743105, 743857, 743193, 744075, 691357, 653165, 678756, 751536, 667273, 667274, 668048, 668555, 669831, 670723, 667461, 670762, 667046, 729450, 729656, 94776, 114253, 114258, 114264, 114279, 650588, 714025, 717004, 650907, 692398, 664391, 655657, 679965, 749601, 751980, 710686, 393286, 750893, 749475, 326273, 326358, 171236, 681772, 701882, 136307, 136315, 707347, 716839, 208697, 171764, 288813, 288816, 288824, 288826, 288829, 288830, 288834, 288836, 288837, 288841, 288842, 136638, 136639, 136785, 729532, 136948, 136949, 171762, 171763, 171765, 678084, 649347, 30556, 30572, 665152
18 amino acids in the Nterminus function as a signal peptide that aides in the secretion of the enzyme
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38% of glucose oxidase activity in the stationary phase and 46% of glucose oxidase activity in the mid-exponential phase is localised in the extracellular fluid
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the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
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variation in the number of isoforms, depending on culture medium used, due to proteolytic cleveage of a single polypeptide
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389419, 389421, 389792, 672763, 678756, 749601, 393286, 393345, 288826, 288835, 288843, 26100, 208564, 208567, 649347
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34% of glucose oxidase activity in the stationary phase and 26% of glucose oxidase activity in the mid-exponential phase is localised in the membrane
the enzyme has no N-terminal membrane anchor in contrast to the microsomal epoxide hydrolase, 3.3.2.9
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additional information
N-terminal mitochondrial signal and C-terminal peroxisomal target sequence, unclear if both are functional
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LINKS TO OTHER DATABASES (specific for Aspergillus niger)
SILVA: 16S/18S rRNA, 23S/28S rRNA
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