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cpdB cpdB cobB cobB ppnK ppnK cinA cinA deoD deoD AJF85585.1 AJF85585.1 nadD nadD nadA nadA nadC nadC nadB nadB ppnK-2 ppnK-2 AJF87781.1 AJF87781.1 AJF86305.1 AJF86305.1 nadE nadE gabD gabD
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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
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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cpdB2', 3'-cyclic nucleotide 2'-phosphodiesterase; In Escherichia coli this is a periplasmic enzyme while in gram positive organisms it may be anchored at the cell surface; this protein appears to consist of a dimer fusion; functions during ribonucleic acid degradation; 2',3'-cyclic nucleotides are first converted to 3'-nucleotide and then cleaved to yield a ribonucleotide and a phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology. (1449 aa)
cobBNAD-dependent deacetylase; NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form; Belongs to the sirtuin family. Class U subfamily. (247 aa)
ppnKInorganic polyphosphate kinase; Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. (266 aa)
cinADamage-inducible protein CinA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the CinA family. (416 aa)
deoDPurine nucleoside phosphorylase DeoD-type; Derived by automated computational analysis using gene prediction method: Protein Homology. (232 aa)
AJF85585.1Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. (271 aa)
nadDNicotinate-nucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). (189 aa)
nadAQuinolinate synthetase; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. (368 aa)
nadCNicotinate-nucleotide pyrophosphorylase; Catalyzes the formation of pyridine-2,3-dicarboxylate and 5-phospho-alpha-D-ribose 1-diphosphate from nictinate D-ribonucleotide; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the NadC/ModD family. (286 aa)
nadBL-aspartate oxidase; Catalyzes the oxidation of L-aspartate to iminoaspartate. (522 aa)
ppnK-2Inorganic polyphosphate kinase; Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. (267 aa)
AJF87781.1Nicotinate phosphoribosyltransferase; Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D- ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Belongs to the NAPRTase family. (487 aa)
AJF86305.15'-nucleotidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the 5'-nucleotidase family. (462 aa)
nadENAD synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source; Belongs to the NAD synthetase family. (272 aa)
gabDSuccinate-semialdehyde dehydrogenase; Catalyzes the formation of succinate from succinate semialdehyde; NADP dependent; Derived by automated computational analysis using gene prediction method: Protein Homology. (462 aa)
Your Current Organism:
Bacillus atrophaeus
NCBI taxonomy Id: 1452
Other names: ATCC 49337, B. atrophaeus, Bacillus atriphaeus, Bacillus sp. S2 BC-2, Bacillus subtilis DSM 2277, Bacillus subtilis DSM 675, CCUG 28524, CIP 107159, DSM 7264, IFO 15539, JCM 9070, LMG 16797, LMG:16797, NBRC 15539, NRRL NRS-213
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