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acnB acnB cyoE cyoE cyoD cyoD cyoC cyoC cyoB cyoB cyoA cyoA aes aes gltA gltA STM0731 STM0731 sdhC sdhC sdhD sdhD sdhA sdhA sdhB sdhB sucA sucA sucB sucB sucC sucC sucD sucD STM0761 STM0761 STM0762 STM0762 aspC aspC icdA icdA orf70 orf70 fumA fumA fumC fumC sfcA sfcA nifJ nifJ acnA acnA nuoN nuoN nuoM nuoM nuoL nuoL nuoK nuoK nuoJ nuoJ nuoI nuoI nuoH nuoH nuoG nuoG nuoF nuoF nuoE nuoE nuoC nuoC nuoB nuoB nuoA nuoA yfbQ yfbQ yfhL yfhL yraR yraR STM3354 STM3354 STM3355 STM3355 mdh mdh yhjJ yhjJ fumB fumB frdD frdD frdC frdC frdB frdB frdA frdA
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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acnBAconitate hydratase 2; Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2- methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a RNA- binding regulatory protein which regulates FliC synthesis via interaction with the ftsH transcript to decrease the intracellular levels of FtsH. The lower levels of Fts [...] (865 aa)
cyoEProtohaeme IX farnesyltransferase (haeme O biosynthesis); Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. (296 aa)
cyoDSimilar to E. coli cytochrome o ubiquinol oxidase subunit IV (AAC73532.1); Blastp hit to AAC73532.1 (109 aa), 93% identity in aa 1 - 109. (109 aa)
cyoCSimilar to E. coli cytochrome o ubiquinol oxidase subunit III (AAC73533.1); Blastp hit to AAC73533.1 (204 aa), 96% identity in aa 1 - 204. (204 aa)
cyoBSimilar to E. coli cytochrome o ubiquinol oxidase subunit I (AAC73534.1); Blastp hit to AAC73534.1 (663 aa), 95% identity in aa 1 - 663; Belongs to the heme-copper respiratory oxidase family. (663 aa)
cyoASimilar to E. coli cytochrome o ubiquinol oxidase subunit II (AAC73535.1); Blastp hit to AAC73535.1 (315 aa), 95% identity in aa 1 - 315. (318 aa)
aesAcetyl esterase; Displays esterase activity towards short chain fatty esters (acyl chain length of up to 8 carbons). Able to hydrolyze triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but not trioleylglycerol (triolein) or cholesterol oleate. Negatively regulates MalT activity by antagonizing maltotriose binding. Inhibits MelA galactosidase activity. (323 aa)
gltACitrate synthase. (SW:CISY_SALTY). (427 aa)
STM0731Putative inner membrane protein. (128 aa)
sdhCSuccinate dehydrogenase, cytochrome b556; Membrane-anchoring subunit of succinate dehydrogenase (SDH). (129 aa)
sdhDSuccinate dehydrogenase, hydrophobic subunit; Membrane-anchoring subunit of succinate dehydrogenase (SDH). (115 aa)
sdhASuccinate dehydrogenase, flavoprotein subunit; Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (588 aa)
sdhBSuccinate dehydrogenase, Fe-S protein; Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. (239 aa)
sucASimilar to E. coli 2-oxoglutarate dehydrogenase (decarboxylase component) (AAC73820.1); Blastp hit to AAC73820.1 (933 aa), 94% identity in aa 1 - 933. (933 aa)
sucB2-oxoglutarate dehydrogenase (dihydrolipoyltranssuccinase E2 component); 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). (402 aa)
sucCsuccinyl-CoA synthetase, beta subunit; 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. (388 aa)
sucDsuccinyl-CoA synthetase, alpha subunit; 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. (289 aa)
STM0761Similar to E. coli fumarase B= fumarate hydratase Class I; anaerobic isozyme (AAC77083.1); Blastp hit to AAC77083.1 (548 aa), 36% identity in aa 361 - 541. (181 aa)
STM0762Similar to E. coli L-tartrate dehydratase, subunit A (AAC76097.1); Blastp hit to AAC76097.1 (303 aa), 29% identity in aa 29 - 287. (281 aa)
aspCSimilar to E. coli aspartate aminotransferase (AAC74014.1); Blastp hit to AAC74014.1 (396 aa), 95% identity in aa 1 - 396; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (396 aa)
icdAIsocitrate dehydrogenase in e14 prophage; Specific for NADP+; similar to E. coli isocitrate dehydrogenase, specific for NADP+ (AAC74220.1); Blastp hit to AAC74220.1 (416 aa), 96% identity in aa 1 - 416. (416 aa)
orf70Putative cytoplasmic protein; In vitro catalyzes the addition of water to fumarate, forming malate. Cannot catalyze the reverse reaction. Cannot use the cis-isomer maleate as substrate; Belongs to the FumD family. (70 aa)
fumAFumarase A; Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate. (548 aa)
fumCFumarase C; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. (467 aa)
sfcASimilar to E. coli NAD-linked malate dehydrogenase (malic enzyme) (AAC74552.1); Blastp hit to AAC74552.1 (574 aa), 92% identity in aa 10 - 574; Belongs to the malic enzymes family. (565 aa)
nifJSimilar to E. coli putative oxidoreductase, Fe-S subunit (AAC74460.1); Blastp hit to AAC74460.1 (1174 aa), 92% identity in aa 1 - 1174. (1174 aa)
acnAAconitate hydratase 1; Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2- methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The (2S,3S)-2-methylcitrate (2-MC) is a very poor substrate. The apo form of AcnA functions as a RNA-binding regulatory protein (By similarity). Belongs to the aconitase/IPM isomerase family. (891 aa)
nuoNNADH dehydrogenase I chain 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. (425 aa)
nuoMSimilar to E. coli NADH dehydrogenase I chain M (AAC75337.1); Blastp hit to AAC75337.1 (509 aa), 96% identity in aa 1 - 509. (509 aa)
nuoLSimilar to E. coli NADH dehydrogenase I chain L (AAC75338.1); Blastp hit to AAC75338.1 (613 aa), 94% identity in aa 1 - 613. (613 aa)
nuoKNADH dehydrogenase I chain 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. (100 aa)
nuoJNADH dehydrogenase I chain J; 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. (184 aa)
nuoINADH dehydrogenase I chain 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. (180 aa)
nuoHNADH dehydrogenase I chain 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. (325 aa)
nuoGNADH dehydrogenase I chain G; 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 (By similarity). (910 aa)
nuoFNADH dehydrogenase I chain F; 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 (By similarity). (445 aa)
nuoENADH dehydrogenase I chain E; 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 (By similarity); Belongs to the complex I 24 kDa subunit family. (166 aa)
nuoCNADH dehydrogenase I chain C,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; In the N-terminal section; belongs to the complex I 30 kDa subunit family. (600 aa)
nuoBNADH dehydrogenase I chain B; 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. (220 aa)
nuoANADH dehydrogenase I chain A; 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 3 family. (147 aa)
yfbQPutative regulator; similar to E. coli putative aminotransferase (AAC75350.1); Blastp hit to AAC75350.1 (405 aa), 96% identity in aa 1 - 404. (404 aa)
yfhLPutative ferredoxin; Similar to E. coli orf, hypothetical protein (AAC75615.1); Blastp hit to AAC75615.1 (86 aa), 94% identity in aa 1 - 86. (86 aa)
yraRPutative nucleoside-diphosphate-sugar epimerase; Similar to E. coli orf, hypothetical protein (AAC76186.1); Blastp hit to AAC76186.1 (226 aa), 86% identity in aa 6 - 226. (222 aa)
STM3354Similar to E. coli L-tartrate dehydratase, subunit B (AAC76098.1); Blastp hit to AAC76098.1 (201 aa), 69% identity in aa 2 - 201. (205 aa)
STM3355Similar to E. coli L-tartrate dehydratase, subunit A (AAC76097.1); Blastp hit to AAC76097.1 (303 aa), 54% identity in aa 6 - 299. (299 aa)
mdhMalate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. (312 aa)
yhjJPutative Zn-dependent peptidase; Protein YHJJ precursor. (SW:YHJJ_SALTY); Belongs to the peptidase M16 family. (495 aa)
fumBFumarase B; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family. (548 aa)
frdDFumarate reductase; Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. (119 aa)
frdCFumarate reductase; Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. (131 aa)
frdBFumarate reductase; Anaerobic; Fe-S protein subunit; similar to E. coli fumarate reductase, anaerobic, iron-sulfur protein subunit (AAC77113.1); Blastp hit to AAC77113.1 (244 aa), 95% identity in aa 1 - 244; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (244 aa)
frdAFumarate reductase; Anaerobic; flavoprotein subunit; similar to E. coli fumarate reductase, anaerobic, flavoprotein subunit (AAC77114.1); Blastp hit to AAC77114.1 (602 aa), 95% identity in aa 1 - 595. (596 aa)
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
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