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glcB glcB APE07920.1 APE07920.1 APE11968.1 APE11968.1 sucC sucC sucD sucD aspA aspA kgd kgd APE12034.1 APE12034.1 APE08376.1 APE08376.1 acnA acnA APE08640.1 APE08640.1 mqo mqo APE08831.1 APE08831.1 APE12100.1 APE12100.1 ppc ppc APE09032.1 APE09032.1 mqo-2 mqo-2 APE09141.1 APE09141.1 nuoN nuoN APE09461.1 APE09461.1 APE09462.1 APE09462.1 nuoK nuoK nuoI nuoI nuoH nuoH APE09467.1 APE09467.1 APE12171.1 APE12171.1 APE09522.1 APE09522.1 APE09581.1 APE09581.1 APE09589.1 APE09589.1 APE09591.1 APE09591.1 APE12196.1 APE12196.1 APE09847.1 APE09847.1 APE09990.1 APE09990.1 APE10015.1 APE10015.1 APE10016.1 APE10016.1 APE10018.1 APE10018.1 APE10023.1 APE10023.1 APE10310.1 APE10310.1 BO226_14850 BO226_14850 APE10354.1 APE10354.1 APE10410.1 APE10410.1 APE10677.1 APE10677.1 APE10678.1 APE10678.1 APE12512.1 APE12512.1 APE11940.1 APE11940.1
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:
glcBMalate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily. (727 aa)
APE07920.1Citrate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the citrate synthase family. (375 aa)
APE11968.1Citrate (Si)-synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the citrate synthase family. (413 aa)
sucCsuccinate--CoA ligase 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. (389 aa)
sucDsuccinate--CoA ligase subunit alpha; 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. (300 aa)
aspAAspartate ammonia-lyase; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. (471 aa)
kgdAlpha-ketoglutarate decarboxylase; Kgd; produces succinic semialdehyde; part of alternative pathway from alpha-ketoglutarate to succinate; essential for normal growth; Derived by automated computational analysis using gene prediction method: Protein Homology. (1240 aa)
APE12034.1Hydroxyglutarate oxidase; Catalyzed the formation of 2-ketoglutarate from 2-hydroxyglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology. (398 aa)
APE08376.1Cytochrome c oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (582 aa)
acnAAconitate hydratase; Catalyzes the conversion of citrate to isocitrate; Derived by automated computational analysis using gene prediction method: Protein Homology. (932 aa)
APE08640.14Fe-4S ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (303 aa)
mqoMalate:quinone oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (497 aa)
APE08831.1Cyclase; Derived by automated computational analysis using gene prediction method: Protein Homology. (146 aa)
APE12100.1Molybdopterin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (761 aa)
ppcPhosphoenolpyruvate carboxylase; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle; Belongs to the PEPCase type 1 family. (920 aa)
APE09032.1Aconitate hydratase 1; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate. (934 aa)
mqo-2Malate dehydrogenase (acceptor); Derived by automated computational analysis using gene prediction method: Protein Homology. (501 aa)
APE09141.1Isocitrate dehydrogenase (NADP(+)); Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the monomeric-type IDH family. (752 aa)
nuoNNADH-quinone oxidoreductase subunit N; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 2 family. (534 aa)
APE09461.1NADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (563 aa)
APE09462.1NADH-quinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. (630 aa)
nuoKNADH-quinone oxidoreductase subunit K; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 4L family. (99 aa)
nuoINADH-quinone oxidoreductase subunit I; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (181 aa)
nuoHNADH-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. (433 aa)
APE09467.1NADH-quinone oxidoreductase subunit G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. (822 aa)
APE12171.1NADH oxidoreductase (quinone) subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. (435 aa)
APE09522.1Succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. (248 aa)
APE09581.1Polyketide cyclase / dehydrase and lipid transport; Derived by automated computational analysis using gene prediction method: Protein Homology. (134 aa)
APE09589.1Derived by automated computational analysis using gene prediction method: Protein Homology. (204 aa)
APE09591.1Derived by automated computational analysis using gene prediction method: Protein Homology. (553 aa)
APE12196.12-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. (583 aa)
APE09847.1Cytochrome c oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (555 aa)
APE09990.1FAD-binding oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (456 aa)
APE10015.1Succinate dehydrogenase, cytochrome b556 subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. (111 aa)
APE10016.1Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (146 aa)
APE10018.1Succinate dehydrogenase iron-sulfur subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. (258 aa)
APE10023.1Isocitrate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the isocitrate and isopropylmalate dehydrogenases family. (405 aa)
APE10310.1Isocitrate lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. (429 aa)
BO226_14850Transcriptional regulator; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. (467 aa)
APE10354.1Na+/H+ antiporter subunit D; Derived by automated computational analysis using gene prediction method: Protein Homology. (529 aa)
APE10410.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (81 aa)
APE10677.12-oxoacid:ferredoxin oxidoreductase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology. (356 aa)
APE10678.12-oxoglutarate ferredoxin oxidoreductase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology. (644 aa)
APE12512.1Cytochrome ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (499 aa)
APE11940.1Cytochrome d ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (345 aa)
Your Current Organism:
Rhodococcus sp. 2G
NCBI taxonomy Id: 1570939
Other names: R. sp. 2G
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