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ppc ppc frdB frdB aspA aspA aceK aceK aceA aceA aceB aceB ubiE ubiE mdh mdh hycF hycF nuoB nuoB nuoG nuoG nuoH nuoH nuoI nuoI nuoK nuoK nuoL nuoL nuoM nuoM nuoN nuoN STM1793 STM1793 STM1792 STM1792 acnA acnA fumC fumC fumA fumA icdA icdA cydB cydB cydA cydA sucD sucD sucC sucC sucB sucB sucA sucA sdhB sdhB sdhA sdhA sdhD sdhD sdhC sdhC gltA gltA fdrA fdrA cyoA cyoA cyoB cyoB cyoC cyoC cyoD cyoD prpD prpD prpC prpC STM0361 STM0361 STM0360 STM0360 acnB acnB
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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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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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experimentally determined
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gene neighborhood
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ppcPhosphoenolpyruvate carboxylase; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. (883 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)
aspASimilar to E. coli aspartate ammonia-lyase (aspartase) (AAC77099.1); Blastp hit to AAC77099.1 (493 aa), 97% identity in aa 16 - 493. (478 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. (583 aa)
aceAIsocitrate lyase; Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates. (434 aa)
aceBSimilar to E. coli malate synthase A (AAC76984.1); Blastp hit to AAC76984.1 (533 aa), 90% identity in aa 1 - 533. (533 aa)
ubiES-adenosylmethionine; 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). (251 aa)
mdhMalate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. (312 aa)
hycFHydrogenase 3; Similar to E. coli probable iron-sulfur protein of hydrogenase 3 (part of FHL complex) (AAC75762.1); Blastp hit to AAC75762.1 (180 aa), 96% identity in aa 1 - 178; putative quinone oxidoreductase. (180 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)
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)
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)
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)
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)
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)
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)
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)
STM1793Similar to E. coli probable third cytochrome oxidase, subunit II (AAC74064.1); Blastp hit to AAC74064.1 (378 aa), 80% identity in aa 1 - 378. (378 aa)
STM1792Similar to E. coli probable third cytochrome oxidase, subunit I (AAC74063.1); Blastp hit to AAC74063.1 (514 aa), 88% identity in aa 1 - 514. (514 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)
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)
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)
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)
cydBSimilar to E. coli cytochrome d terminal oxidase polypeptide subunit II (AAC73828.1); Blastp hit to AAC73828.1 (379 aa), 92% identity in aa 1 - 379. (379 aa)
cydASimilar to E. coli cytochrome d terminal oxidase, polypeptide subunit I (AAC73827.1); Blastp hit to AAC73827.1 (523 aa), 96% identity in aa 2 - 523. (522 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)
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)
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)
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)
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)
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)
sdhDSuccinate dehydrogenase, hydrophobic subunit; Membrane-anchoring subunit of succinate dehydrogenase (SDH). (115 aa)
sdhCSuccinate dehydrogenase, cytochrome b556; Membrane-anchoring subunit of succinate dehydrogenase (SDH). (129 aa)
gltACitrate synthase. (SW:CISY_SALTY). (427 aa)
fdrASimilar to E. coli involved in protein transport; multicopy suppressor of dominant negative ftsH mutants (AAC73620.1); Blastp hit to AAC73620.1 (555 aa), 82% identity in aa 1 - 555. (554 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)
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)
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)
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)
prpDPutative protein in propionate catabolism; Involved in the catabolism of short chain fatty acids (SCFA) via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the dehydration of 2-methylcitrate (2-MC) to yield the cis isomer of 2-methyl-aconitate. It is also able to catalyze the dehydration of citrate at a lower rate, and the hydration of cis- aconitate. It has no aconitase-like activity and is unable to catalyze the hydration of 2-methyl-cis-aconitate. (483 aa)
prpCPutative citrate synthase; Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA or butyryl-CoA but with a lower specificity. (389 aa)
STM0361Cytochrome BD2 subunit II; Similar to E. coli cytochrome d terminal oxidase polypeptide subunit II (AAC73828.1); Blastp hit to AAC73828.1 (379 aa), 34% identity in aa 7 - 221, 22% identity in aa 121 - 366. (336 aa)
STM0360Similar to E. coli probable third cytochrome oxidase, subunit I (AAC74063.1); Blastp hit to AAC74063.1 (514 aa), 38% identity in aa 2 - 316, 38% identity in aa 381 - 512. (467 aa)
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)
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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