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gcdH gcdH gabD-I gabD-I gabT gabT davA davA davB davB PP_0582 PP_0582 patD patD PP_1845 PP_1845 fadA fadA fadB fadB PP_2215 PP_2215 PP_2217 PP_2217 sad-I sad-I prr prr csiD csiD lhgO lhgO paaF paaF PP_3355 PP_3355 dpkA dpkA bktB bktB PP_4030 PP_4030 lpdG lpdG sucB sucB lpdV lpdV gabD-II gabD-II yqeF yqeF amaB amaB lpd lpd
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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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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
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gcdHglutaryl-CoA dehydrogenase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Energy metabolism. (393 aa)
gabD-ISuccinate-semialdehyde dehydrogenase (NADP+); Catalyzes the conversion of 5-oxopentanoate (glutarate semialdehyde) to glutarate. Involved in L-lysine degradation. (480 aa)
gabT4-aminobutyrate aminotransferase; Catalyzes the conversion of 5-aminovalerate to 5- oxopentanoate. (425 aa)
davA5-aminopentanamidase; Function experimentally demonstrated in the studied strain; enzyme; Energymetabolism : Amino acids and amines. (264 aa)
davBLysine 2-monooxygenase; Function experimentally demonstrated in the studied strain; enzyme; Energymetabolism : Amino acids and amines. (560 aa)
PP_0582Thiolase family protein; Belongs to the thiolase-like superfamily. Thiolase family. (425 aa)
patDMedium chain aldehyde dehydrogenase; Function experimentally demonstrated in the studied species; enzyme; Energymetabolism : Amino acids and amines; Belongs to the aldehyde dehydrogenase family. (474 aa)
PP_1845Enoyl-CoA hydratase/isomerase family protein. (229 aa)
fadA3-ketoacyl-CoA thiolase (thiolase I); Function of strongly homologous gene; enzyme; Belongs to the thiolase-like superfamily. Thiolase family. (394 aa)
fadBenoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. (715 aa)
PP_2215acetyl-CoA acetyltransferase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Fattyacidandphospholipidmetabolism : Degradation; Belongs to the thiolase-like superfamily. Thiolase family. (397 aa)
PP_2217enoyl-CoA hydratase; Function experimentally demonstrated in the studied species; enzyme; Energy metabolism; Belongs to the enoyl-CoA hydratase/isomerase family. (257 aa)
sad-INAD+-dependent succinate semialdehyde dehydrogenase; Function experimentally demonstrated in the studied genus; enzyme; Biologicalprocesses : Scavenge (Catabolism). (463 aa)
prrGamma-aminobutyraldehyde dehydrogenase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the aldehyde dehydrogenase family. (474 aa)
csiDCarbon starvation induced protein; Acts as an alpha-ketoglutarate-dependent dioxygenase catalyzing hydroxylation of glutarate (GA) to L-2-hydroxyglutarate (L2HG). Functions in a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. (325 aa)
lhgOL-2-hydroxyglutarate oxidase; Function experimentally demonstrated in the studied genus; enzyme; Energy metabolism. (416 aa)
paaFenoyl-CoA hydratase-isomerase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Biologicalprocesses : Scavenge (Catabolism); Belongs to the enoyl-CoA hydratase/isomerase family. (257 aa)
PP_3355Beta-ketothiolase; Belongs to the thiolase-like superfamily. Thiolase family. (396 aa)
dpkADelta 1-piperideine-2-carboxylate reductase; Function experimentally demonstrated in the studied strain; enzyme; Energymetabolism : Amino acids and amines; Belongs to the LDH2/MDH2 oxidoreductase family. (332 aa)
bktBBeta-ketothiolase BktB; Belongs to the thiolase-like superfamily. Thiolase family. (394 aa)
PP_4030Enoyl-CoA hydratase/isomerase family protein; Belongs to the enoyl-CoA hydratase/isomerase family. (280 aa)
lpdGDihydrolipoyl dehydrogenase; Function experimentally demonstrated in the studied species; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Folic acid. (478 aa)
sucB2-oxoglutarate dehydrogenase dihydrolipoyltranssuccinylase subunit; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2). (407 aa)
lpdVDihydrolipoyl dehydrogenase component of branched-chain alpha-keto acid dehydrogenase complex; Function experimentally demonstrated in the studied species; enzyme; Fattyacidandphospholipidmetabolism : Degradation. (459 aa)
gabD-IISuccinate-semialdehyde dehydrogenase (NADP+); Function experimentally demonstrated in the studied species; enzyme; Energymetabolism : Amino acids and amines. (490 aa)
yqeFacetyl-CoA acetyltransferase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Fattyacidandphospholipidmetabolism : Degradation; Belongs to the thiolase-like superfamily. Thiolase family. (392 aa)
amaBL-piperidine-6-carboxylate dehydrogenase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Energymetabolism : Amino acids and amines; Belongs to the aldehyde dehydrogenase family. (496 aa)
lpdDihydrolipoyl dehydrogenase; Function experimentally demonstrated in the studied species; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Folic acid. (466 aa)
Your Current Organism:
Pseudomonas putida KT2440
NCBI taxonomy Id: 160488
Other names: P. putida KT2440, Pseudomonas putida (strain KT2440), Pseudomonas putida str. KT2440
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