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W6QNF6_PENRF W6QNF6_PENRF W6QLX1_PENRF W6QLX1_PENRF W6QL01_PENRF W6QL01_PENRF W6QIU5_PENRF W6QIU5_PENRF mpaA mpaA coq5 coq5 MOD-E MOD-E W6QCZ5_PENRF W6QCZ5_PENRF W6R2J2_PENRF W6R2J2_PENRF W6R2A8_PENRF W6R2A8_PENRF COQ3 COQ3 W6QVX8_PENRF W6QVX8_PENRF W6QV23_PENRF W6QV23_PENRF W6QRF5_PENRF W6QRF5_PENRF W6QQJ7_PENRF W6QQJ7_PENRF W6QPN1_PENRF W6QPN1_PENRF COQ2 COQ2 W6QEH4_PENRF W6QEH4_PENRF W6QDV5_PENRF W6QDV5_PENRF cprA cprA W6QA69_PENRF W6QA69_PENRF W6QPK4_PENRF W6QPK4_PENRF COQ6 COQ6 W6QNG4_PENRF W6QNG4_PENRF W6QF77_PENRF W6QF77_PENRF W6Q8N6_PENRF W6Q8N6_PENRF W6Q8A9_PENRF W6Q8A9_PENRF W6Q7W9_PENRF W6Q7W9_PENRF icdA icdA W6Q6S7_PENRF W6Q6S7_PENRF W6Q5S3_PENRF W6Q5S3_PENRF W6Q3Y1_PENRF W6Q3Y1_PENRF W6Q2Q0_PENRF W6Q2Q0_PENRF W6Q005_PENRF W6Q005_PENRF W6PZK5_PENRF W6PZK5_PENRF W6PWR6_PENRF W6PWR6_PENRF W6PWD4_PENRF W6PWD4_PENRF W6PRD3_PENRF W6PRD3_PENRF
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:
W6QNF6_PENRFFlavin_Reduct domain-containing protein. (301 aa)
W6QLX1_PENRFUncharacterized protein. (69 aa)
W6QL01_PENRFGenomic scaffold, ProqFM164S03. (112 aa)
W6QIU5_PENRF4-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. (335 aa)
mpaAPolyprenyl transferase mapA; Polyprenyl transferase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world. The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHDMP) by mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure [...] (325 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). (314 aa)
MOD-EHeat shock protein 90 homolog. (698 aa)
W6QCZ5_PENRFGTP cyclohydrolase I. (78 aa)
W6R2J2_PENRFGenomic scaffold, ProqFM164S04. (71 aa)
W6R2A8_PENRFAromatic-ring hydroxylase-like. (666 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. (358 aa)
W6QVX8_PENRFUncharacterized protein. (338 aa)
W6QV23_PENRFAromatic-ring hydroxylase-like. (599 aa)
W6QRF5_PENRFFlavodoxin. (658 aa)
W6QQJ7_PENRFAromatic-ring hydroxylase-like. (525 aa)
W6QPN1_PENRFUncharacterized protein. (289 aa)
COQ24-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)
W6QEH4_PENRFShort-chain dehydrogenase/reductase SDR. (253 aa)
W6QDV5_PENRFGenomic scaffold, ProqFM164S02. (330 aa)
cprANADPH--cytochrome P450 reductase; This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis. In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. (695 aa)
W6QA69_PENRFAromatic-ring hydroxylase-like. (634 aa)
W6QPK4_PENRFMonooxygenase, FAD-binding. (135 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)
W6QNG4_PENRFAromatic-ring hydroxylase-like. (353 aa)
W6QF77_PENRFAromatic-ring hydroxylase-like. (611 aa)
W6Q8N6_PENRFProbable hexaprenyl pyrophosphate synthase, mitochondrial; Belongs to the FPP/GGPP synthase family. (447 aa)
W6Q8A9_PENRFUncharacterized protein. (285 aa)
W6Q7W9_PENRFUbiquinone biosynthesis protein Coq7. (139 aa)
icdAIsocitrate dehydrogenase [NADP]; Belongs to the isocitrate and isopropylmalate dehydrogenases family. (412 aa)
W6Q6S7_PENRFAromatic-ring hydroxylase-like. (200 aa)
W6Q5S3_PENRFGenomic scaffold, ProqFM164S02. (227 aa)
W6Q3Y1_PENRFMethyltransferase type 11. (153 aa)
W6Q2Q0_PENRFZn(2)-C6 fungal-type DNA-binding domain. (562 aa)
W6Q005_PENRFGTP cyclohydrolase I. (344 aa)
W6PZK5_PENRFUbiA prenyltransferase family. (316 aa)
W6PWR6_PENRFUncharacterized protein. (286 aa)
W6PWD4_PENRFUncharacterized protein. (659 aa)
W6PRD3_PENRFMethyltransferase type 11. (264 aa)
Your Current Organism:
Penicillium roqueforti
NCBI taxonomy Id: 1365484
Other names: P. roqueforti FM164, Penicillium roqueforti FM164
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