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gltA gltA AMN48302.1 AMN48302.1 ubiE ubiE AMN47741.1 AMN47741.1 AMN47736.1 AMN47736.1 AMN47312.1 AMN47312.1 AMN47311.1 AMN47311.1 AMN47310.1 AMN47310.1 AMN47309.1 AMN47309.1 AMN47161.1 AMN47161.1 acnA acnA fumC fumC nuoN nuoN AMN46837.1 AMN46837.1 AMN46836.1 AMN46836.1 nuoK nuoK nuoI nuoI nuoH nuoH AMN46831.1 AMN46831.1 AMN46829.1 AMN46829.1 nuoD nuoD AMN46804.1 AMN46804.1 AMN46738.1 AMN46738.1 AMN46424.1 AMN46424.1 AMN46132.1 AMN46132.1 AMN46080.1 AMN46080.1 aceK aceK AMN46042.1 AMN46042.1 AMN45999.1 AMN45999.1 AMN45996.1 AMN45996.1 AMN45939.1 AMN45939.1 AMN45937.1 AMN45937.1 glcB glcB AMN45638.1 AMN45638.1 AMN48443.1 AMN48443.1 AMN48444.1 AMN48444.1 AMN48446.1 AMN48446.1 AMN47789.1 AMN47789.1 AMN47751.1 AMN47751.1 sucD sucD ppc ppc sucC sucC AMN47925.1 AMN47925.1 AMN48047.1 AMN48047.1 mdh mdh
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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gltA'type 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'; Belongs to the citrate synthase family. (432 aa)
AMN48302.1Hypothetical protein. (450 aa)
ubiEUbiquinone biosynthesis methyltransferase UbiE; Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3- methyl-6-methoxy-1,4-benzoquinol (DMQH2). (257 aa)
AMN47741.1Cytochrome oxidase subunit I. (566 aa)
AMN47736.1Cytochrome C oxidase subunit I. (487 aa)
AMN47312.1Fumarate reductase, cytochrome b subunit. (137 aa)
AMN47311.1Fumarate reductase, membrane anchor subunit. (131 aa)
AMN47310.1Succinate dehydrogenase / fumarate reductase, flavoprotein subunit; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (594 aa)
AMN47309.1Succinate dehydrogenase / fumarate reductase, iron-sulfur subunit; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (260 aa)
AMN47161.12-oxoglutarate dehydrogenase E1 component. (970 aa)
acnAAconitate hydratase; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate. (896 aa)
fumCFumarate hydratase, class II; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. (470 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 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; Belongs to the complex I subunit 2 family. (478 aa)
AMN46837.1NADH-quinone oxidoreductase subunit M. (509 aa)
AMN46836.1NADH-quinone oxidoreductase subunit L. (671 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 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; Belongs to the complex I subunit 4L family. (101 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. (144 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. (350 aa)
AMN46831.1NADH dehydrogenase; 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. (747 aa)
AMN46829.1NADH-quinone oxidoreductase subunit E. (179 aa)
nuoDNADH-quinone oxidoreductase subunit D; 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; Belongs to the complex I 49 kDa subunit family. (417 aa)
AMN46804.1Hypothetical protein. (145 aa)
AMN46738.1Electron transfer flavoprotein-ubiquinone oxidoreductase; Accepts electrons from ETF and reduces ubiquinone. (536 aa)
AMN46424.1Hypothetical protein. (622 aa)
AMN46132.1Cytochrome B; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (406 aa)
AMN46080.1Converts isocitrate to alpha ketoglutarate. (432 aa)
aceKIsocitrate dehydrogenase kinase/phosphatase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. (595 aa)
AMN46042.1Nitric oxide reductase NorB. (562 aa)
AMN45999.1Cbb3-type cytochrome c oxidase subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (326 aa)
AMN45996.1Cbb3-type cytochrome c oxidase subunit I; CcoN; FixN; Belongs to the heme-copper respiratory oxidase family. (492 aa)
AMN45939.1'subunit A of antiporter complex involved in resistance to high concentrations of Na+, K+, Li+ and/or alkali; in S. meliloti it is known to be involved with K+'. (970 aa)
AMN45937.1'subunit D of antiporter complex involved in resistance to high concentrations of Na+, K+, Li+ and/or alkali; contains an oxidoreductase domain; catalyzes the transfer of electrons from NADH to ubiquinone'. (552 aa)
glcBMalate synthase; 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. (720 aa)
AMN45638.1Hypothetical protein. (185 aa)
AMN48443.1Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (276 aa)
AMN48444.1Cytochrome 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. (533 aa)
AMN48446.1Cytochrome c oxidase subunit III. (294 aa)
AMN47789.1Hypothetical protein. (422 aa)
AMN47751.1Hypothetical protein. (472 aa)
sucDsuccinyl-CoA synthetase 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. (398 aa)
ppcPhosphoenolpyruvate carboxylase; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle; Belongs to the PEPCase type 1 family. (910 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. (387 aa)
AMN47925.1Methylamine---corrinoid protein Co-methyltransferase. (449 aa)
AMN48047.1Cytochrome B561. (184 aa)
mdhMalate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. Belongs to the LDH/MDH superfamily. MDH type 2 family. (325 aa)
Your Current Organism:
Steroidobacter denitrificans
NCBI taxonomy Id: 465721
Other names: DSM 18526, JCM 14622, S. denitrificans, Steroidobacter denitrificans Fahrbach et al. 2008, gamma proteobacterium FS-2007, strain FS
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