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ALL04127.1 ALL04127.1 ALL04539.1 ALL04539.1 ALL04540.1 ALL04540.1 ALL05090.1 ALL05090.1 sucC sucC aspA aspA gltA gltA sucD sucD ALL08856.1 ALL08856.1 mqo mqo mdh mdh ALL08158.1 ALL08158.1 fumC fumC
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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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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
ALL04127.1Phosphoenolpyruvate carboxylase; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. (863 aa)
ALL04539.12-oxoglutarate dehydrogenase subunit E1; Derived by automated computational analysis using gene prediction method: Protein Homology. (930 aa)
ALL04540.12-oxoglutarate dehydrogenase; 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). (406 aa)
ALL05090.1Isocitrate dehydrogenase; NADP-specific, catalyzes the formation of 2-oxoglutarate from isocitrate or oxalosuccinate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the monomeric-type IDH family. (739 aa)
sucCsuccinyl-CoA synthetase subunit beta; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP 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. (396 aa)
aspAAspartate ammonia-lyase; Catalyzes the formation of fumarate from aspartate; Derived by automated computational analysis using gene prediction method: Protein Homology. (469 aa)
gltAType II enzyme; in Escherichia coli this enzyme forms a trimer of dimers which is allosterically inhibited by NADH and competitively inhibited by alpha-ketoglutarate; allosteric inhibition is lost when Cys206 is chemically modified which also affects hexamer formation; forms oxaloacetate and acetyl-CoA and water from citrate and coenzyme A; functions in TCA cycle, glyoxylate cycle and respiration; enzyme from Helicobacter pylori is not inhibited by NADH; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the citrate synthase family. (428 aa)
sucDsuccinate--CoA ligase; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP 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. (290 aa)
ALL08856.1Converts isocitrate to alpha ketoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the isocitrate and isopropylmalate dehydrogenases family. (411 aa)
mqoMalate:quinone oxidoreductase; Malate dehydrogenase; catalyzes the oxidation of malate to oxaloacetate; Derived by automated computational analysis using gene prediction method: Protein Homology. (501 aa)
mdhMalate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. Belongs to the LDH/MDH superfamily. MDH type 3 family. (312 aa)
ALL08158.1Aconitate hydratase; Derived by automated computational analysis using gene prediction method: Protein Homology. (758 aa)
fumCFumarate hydratase; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. (465 aa)
Your Current Organism:
Pedobacter sp. PACM27299
NCBI taxonomy Id: 1727164
Other names: P. sp. PACM 27299, Pedobacter sp. PACM 27299
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