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A0A1F5LEF6 A0A1F5LEF6 A0A1F5LZ37 A0A1F5LZ37 A0A1F5LX76 A0A1F5LX76 A0A1F5LWB1 A0A1F5LWB1 COQ6 COQ6 A0A1F5LQW2 A0A1F5LQW2 A0A1F5LQ85 A0A1F5LQ85 A0A1F5LQ77 A0A1F5LQ77 COQ4 COQ4 A0A1F5LLV0 A0A1F5LLV0 A0A1F5LKX4 A0A1F5LKX4 A0A1F5LJR2 A0A1F5LJR2 A0A1F5LI85 A0A1F5LI85 COQ3 COQ3 A0A1F5LDX9 A0A1F5LDX9 A0A1F5LAN8 A0A1F5LAN8 COQ7 COQ7 COQ5 COQ5 A0A1F5L640 A0A1F5L640
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.
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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:
A0A1F5LEF6NAD(P)-bd_dom domain-containing protein. (287 aa)
A0A1F5LZ37Uncharacterized protein. (313 aa)
A0A1F5LX76Polyketide_cyc domain-containing protein. (273 aa)
A0A1F5LWB12Fe-2S ferredoxin-type domain-containing protein. (202 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. (509 aa)
A0A1F5LQW2Uncharacterized protein. (240 aa)
A0A1F5LQ85NmrA domain-containing protein. (380 aa)
A0A1F5LQ77Ubiquinone 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. (294 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. (282 aa)
A0A1F5LLV0Uncharacterized protein; Belongs to the FPP/GGPP synthase family. (450 aa)
A0A1F5LKX4NADPH:adrenodoxin oxidoreductase, mitochondrial. (534 aa)
A0A1F5LJR2NmrA domain-containing protein. (331 aa)
A0A1F5LI85Uncharacterized protein. (265 aa)
COQ3Ubiquinone biosynthesis O-methyltransferase, mitochondrial; O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway; Belongs to the class I-like SAM-binding methyltransferase superfamily. UbiG/COQ3 family. (356 aa)
A0A1F5LDX9ABC1 domain-containing protein. (906 aa)
A0A1F5LAN84-hydroxybenzoate polyprenyltransferase, mitochondrial; Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate. (417 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. (241 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). (310 aa)
A0A1F5L640Uncharacterized protein. (253 aa)
Your Current Organism:
Penicillium arizonense
NCBI taxonomy Id: 1835702
Other names: CBS 141311, Herb. C-F-101845, IBT 12289, P. arizonense, Penicillium arizonense Frisvad, Grijseels and J.C. Nielsen, 2016, Penicillium sp. JCN-2016
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