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A0A1F5LUA1 A0A1F5LUA1 A0A1F5L358 A0A1F5L358 A0A1F5L4H7 A0A1F5L4H7 A0A1F5L4X5 A0A1F5L4X5 A0A1F5L5G0 A0A1F5L5G0 A0A1F5L5G4 A0A1F5L5G4 A0A1F5L669 A0A1F5L669 A0A1F5L681 A0A1F5L681 A0A1F5L6E0 A0A1F5L6E0 A0A1F5L6Q7 A0A1F5L6Q7 A0A1F5L6R9 A0A1F5L6R9 A0A1F5L7H2 A0A1F5L7H2 A0A1F5L7M2 A0A1F5L7M2 A0A1F5L805 A0A1F5L805 A0A1F5L818 A0A1F5L818 A0A1F5L8V7 A0A1F5L8V7 A0A1F5L9I2 A0A1F5L9I2 A0A1F5L9W6 A0A1F5L9W6 A0A1F5LAJ9 A0A1F5LAJ9 A0A1F5LAV4 A0A1F5LAV4 A0A1F5LB33 A0A1F5LB33 A0A1F5LD15 A0A1F5LD15 A0A1F5LD29 A0A1F5LD29 A0A1F5LD90 A0A1F5LD90 A0A1F5LDN2 A0A1F5LDN2 A0A1F5LEC7 A0A1F5LEC7 A0A1F5LEL6 A0A1F5LEL6 A0A1F5LFK8 A0A1F5LFK8 A0A1F5LG62 A0A1F5LG62 A0A1F5LGQ2 A0A1F5LGQ2 A0A1F5LHP1 A0A1F5LHP1 A0A1F5LI25 A0A1F5LI25 A0A1F5LIE6 A0A1F5LIE6 A0A1F5LJI6 A0A1F5LJI6 A0A1F5LJW4 A0A1F5LJW4 A0A1F5LL15 A0A1F5LL15 A0A1F5LLP9 A0A1F5LLP9 A0A1F5LLX7 A0A1F5LLX7 A0A1F5LMT4 A0A1F5LMT4 A0A1F5LMV9 A0A1F5LMV9 A0A1F5LNC2 A0A1F5LNC2 A0A1F5LNH8 A0A1F5LNH8 A0A1F5LNN4 A0A1F5LNN4 A0A1F5LNQ2 A0A1F5LNQ2 A0A1F5LPP1 A0A1F5LPP1 A0A1F5LQ22 A0A1F5LQ22 A0A1F5LQG4 A0A1F5LQG4 A0A1F5LQK4 A0A1F5LQK4 A0A1F5LR63 A0A1F5LR63 A0A1F5LRI1 A0A1F5LRI1 A0A1F5LRK8 A0A1F5LRK8 A0A1F5LRL4 A0A1F5LRL4 A0A1F5LRW7 A0A1F5LRW7 A0A1F5LT54 A0A1F5LT54 A0A1F5LTK7 A0A1F5LTK7 A0A1F5LUV9 A0A1F5LUV9 A0A1F5LV57 A0A1F5LV57 A0A1F5LVM3 A0A1F5LVM3 A0A1F5LVW2 A0A1F5LVW2
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
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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
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textmining
co-expression
protein homology
Your Input:
A0A1F5LUA1Citrate synthase; Belongs to the citrate synthase family. (470 aa)
A0A1F5L358Citrate synthase; Belongs to the citrate synthase family. (462 aa)
A0A1F5L4H7MFS domain-containing protein. (520 aa)
A0A1F5L4X5Uncharacterized protein; Belongs to the LDH/MDH superfamily. (301 aa)
A0A1F5L5G0GFA domain-containing protein. (181 aa)
A0A1F5L5G4Transket_pyr domain-containing protein. (1059 aa)
A0A1F5L669Uncharacterized protein. (193 aa)
A0A1F5L681Isocitrate dehydrogenase [NAD] subunit, mitochondrial. (383 aa)
A0A1F5L6E0Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. (443 aa)
A0A1F5L6Q7Uncharacterized protein. (533 aa)
A0A1F5L6R9Pyruvate carboxylase; Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. (1192 aa)
A0A1F5L7H2Acetyltransferase component of pyruvate dehydrogenase complex; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (483 aa)
A0A1F5L7M2WAPL domain-containing protein. (819 aa)
A0A1F5L805Malate dehydrogenase. (340 aa)
A0A1F5L818Uncharacterized protein. (598 aa)
A0A1F5L8V7MFS domain-containing protein. (513 aa)
A0A1F5L9I2Dihydrolipoyl dehydrogenase. (513 aa)
A0A1F5L9W6Iso_dh domain-containing protein. (366 aa)
A0A1F5LAJ9MFS domain-containing protein. (529 aa)
A0A1F5LAV4Kinesin-like protein; Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. (796 aa)
A0A1F5LB33GFA domain-containing protein. (139 aa)
A0A1F5LD15Uncharacterized protein. (275 aa)
A0A1F5LD29GFA domain-containing protein. (136 aa)
A0A1F5LD90MFS domain-containing protein. (1037 aa)
A0A1F5LDN2Uncharacterized protein. (435 aa)
A0A1F5LEC7Pyruvate dehydrogenase E1 component subunit alpha; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (405 aa)
A0A1F5LEL6Bms1-type G domain-containing protein. (802 aa)
A0A1F5LFK8Iso_dh domain-containing protein. (358 aa)
A0A1F5LG62MFS domain-containing protein. (626 aa)
A0A1F5LGQ2Succinate dehydrogenase [ubiquinone] cytochrome b small subunit. (168 aa)
A0A1F5LHP1GFA domain-containing protein. (230 aa)
A0A1F5LI25GFA domain-containing protein. (143 aa)
A0A1F5LIE6Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial; Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). (271 aa)
A0A1F5LJI6Uncharacterized protein. (475 aa)
A0A1F5LJW4MFS domain-containing protein. (513 aa)
A0A1F5LL15Isochorismatase domain-containing protein. (187 aa)
A0A1F5LLP9Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial; Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). (647 aa)
A0A1F5LLX7Lipoyl-binding domain-containing protein. (401 aa)
A0A1F5LMT4Uncharacterized protein. (327 aa)
A0A1F5LMV9ATP-grasp domain-containing protein. (377 aa)
A0A1F5LNC2Uncharacterized protein. (390 aa)
A0A1F5LNH8Isocitrate dehydrogenase [NADP]; Belongs to the isocitrate and isopropylmalate dehydrogenases family. (412 aa)
A0A1F5LNN4Peripheral subunit-binding (PSBD) domain-containing protein. (289 aa)
A0A1F5LNQ2Pyruvate dehydrogenase E1 component subunit beta; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. (375 aa)
A0A1F5LPP1Aconitate hydratase, mitochondrial; Belongs to the aconitase/IPM isomerase family. (791 aa)
A0A1F5LQ22Transket_pyr domain-containing protein. (987 aa)
A0A1F5LQG4Lipoyl-binding domain-containing protein. (442 aa)
A0A1F5LQK4Uncharacterized protein. (485 aa)
A0A1F5LR63Aconitate hydratase, mitochondrial; Belongs to the aconitase/IPM isomerase family. (784 aa)
A0A1F5LRI1Succinate dehydrogenase assembly factor 2, mitochondrial; Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit of the SDH catalytic dimer. (289 aa)
A0A1F5LRK8CoA_binding domain-containing protein. (654 aa)
A0A1F5LRL4MFS domain-containing protein. (566 aa)
A0A1F5LRW7Isocitrate dehydrogenase [NAD] subunit, mitochondrial. (384 aa)
A0A1F5LT54MFS domain-containing protein. (525 aa)
A0A1F5LTK7Uncharacterized protein; Belongs to the LDH/MDH superfamily. (330 aa)
A0A1F5LUV9Uncharacterized protein. (666 aa)
A0A1F5LV57MFS domain-containing protein. (531 aa)
A0A1F5LVM3Succinate--CoA ligase [ADP-forming] subunit alpha, mitochondrial; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. (329 aa)
A0A1F5LVW2Uncharacterized protein. (187 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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