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AB675_5466 AB675_5466 BNA4 BNA4 AB675_2468 AB675_2468 BNA5-2 BNA5-2 BNA5 BNA5 AB675_7037 AB675_7037 AB675_9821 AB675_9821 AB675_8950 AB675_8950
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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Your Input:
AB675_5466Nicotinate-nucleotide pyrophosphorylase [carboxylating]; Involved in the catabolism of quinolinic acid (QA). Belongs to the NadC/ModD family. (310 aa)
BNA4Kynurenine 3-monooxygenase; Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid. (472 aa)
AB675_2468Indoleamine 2,3-dioxygenase. (465 aa)
BNA5-2Kynureninase; Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively; Belongs to the kynureninase family. (489 aa)
BNA5Kynureninase; Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively; Belongs to the kynureninase family. (496 aa)
AB675_7037Indoleamine 2,3-dioxygenase. (436 aa)
AB675_9821Indoleamine 2,3-dioxygenase. (414 aa)
AB675_8950Kynurenine formamidase; Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites. (401 aa)
Your Current Organism:
Phialophora attae
NCBI taxonomy Id: 1664694
Other names: CBS 131958, P. attae, Phialophora attae Attili-Angelis, Duarte, Stielow & de Hoog, 2014
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