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AB675_3236 AB675_3236 AB675_8950 AB675_8950 AB675_9985 AB675_9985 AB675_10313 AB675_10313 AB675_1182 AB675_1182 AB675_10551 AB675_10551 AB675_10569 AB675_10569 AB675_2181 AB675_2181 AB675_6965 AB675_6965 COQ6 COQ6 BNA5 BNA5 AB675_3214 AB675_3214 AB675_22 AB675_22 AB675_11921 AB675_11921 AB675_3888 AB675_3888 AB675_9759 AB675_9759 AB675_1785 AB675_1785 AB675_1765 AB675_1765 COQ4 COQ4 AB675_2377 AB675_2377 BNA5-2 BNA5-2 AB675_6613 AB675_6613 AB675_3839 AB675_3839 AB675_2468 AB675_2468 AB675_881 AB675_881 AB675_1102 AB675_1102 COQ7 COQ7 AB675_10743 AB675_10743 AB675_6921 AB675_6921 AB675_8449 AB675_8449 AB675_2684 AB675_2684 AB675_6536 AB675_6536 AB675_2541 AB675_2541 AB675_48 AB675_48 AB675_1439 AB675_1439 AB675_1181 AB675_1181 AB675_3655 AB675_3655 AB675_9465 AB675_9465 AB675_11299 AB675_11299 COQ5 COQ5 AB675_2117 AB675_2117 AB675_242 AB675_242 BNA4 BNA4
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
AB675_3236ABC1 family protein C10F6.14c. (644 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)
AB675_9985Methyltransf_25 domain-containing protein. (256 aa)
AB675_10313FAD_binding_3 domain-containing protein. (576 aa)
AB675_11823-hydroxybenzoate 6-hydroxylase 1. (191 aa)
AB675_10551Salicylate hydroxylase. (448 aa)
AB675_10569Acyltransferase LovD. (412 aa)
AB675_2181Uncharacterized protein. (187 aa)
AB675_6965FAD_binding_3 domain-containing protein. (452 aa)
COQ6Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial; FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl- 4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via a ferredoxin/ferredoxin reductase system to COQ6. (507 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_32144-hydroxybenzoate polyprenyltransferase, mitochondrial. (358 aa)
AB675_226-hydroxynicotinate 3-monooxygenase. (429 aa)
AB675_11921Beta-lactamase domain-containing protein 2. (402 aa)
AB675_3888FAD_binding_3 domain-containing protein. (410 aa)
AB675_9759Methyltranfer_dom domain-containing protein. (281 aa)
AB675_1785Beta-lactamase domain-containing protein 2. (384 aa)
AB675_1765Acyltransferase LovD. (420 aa)
COQ4Ubiquinone biosynthesis protein COQ4, mitochondrial; Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides; Belongs to the COQ4 family. (303 aa)
AB675_23772-heptyl-3-hydroxy-4(1H)-quinolone synthase. (474 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)
AB675_6613FAD_binding_3 domain-containing protein. (445 aa)
AB675_38392,6-dihydroxypyridine 3-monooxygenase. (426 aa)
AB675_2468Indoleamine 2,3-dioxygenase. (465 aa)
AB675_881NAD(P)-bd_dom domain-containing protein. (296 aa)
AB675_1102FAD_binding_3 domain-containing protein. (443 aa)
COQ75-demethoxyubiquinone hydroxylase, mitochondrial; Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6- methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has also a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides. (272 aa)
AB675_10743Putative aminotransferase. (398 aa)
AB675_6921FAD_binding_3 domain-containing protein. (446 aa)
AB675_8449Beta-lactamase domain-containing protein 2. (392 aa)
AB675_2684Ubiquinone biosynthesis O-methyltransferase, mitochondrial. (230 aa)
AB675_6536ABC1 family protein mitochondrial. (609 aa)
AB675_2541Uncharacterized protein. (269 aa)
AB675_48Uncharacterized protein. (452 aa)
AB675_1439Atypical kinase COQ8, mitochondrial. (780 aa)
AB675_11813-hydroxybenzoate 6-hydroxylase. (279 aa)
AB675_3655ABC1 family protein MCP2. (460 aa)
AB675_94652,6-dihydroxypyridine 3-monooxygenase. (440 aa)
AB675_11299Acyltransferase LovD. (353 aa)
COQ52-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial; Methyltransferase required for the conversion of 2- polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl- 6-methoxy-1,4-benzoquinol (DMQH2). (304 aa)
AB675_2117Ubiquinone biosynthesis protein; Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. (248 aa)
AB675_2426-hydroxynicotinate 3-monooxygenase. (426 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)
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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