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coaBC coaBC coaD coaD panE panE folP folP coaX coaX clpP clpP coaE coaE pyk pyk yuxH yuxH tpiA tpiA panC panC dxr dxr panE-2 panE-2
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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:
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coaBCCoenzyme A biosynthesis bifunctional protein CoaBC; Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'- phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'- phosphopantotheine; In the C-terminal section; belongs to the PPC synthetase family. (406 aa)
coaDPhosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. (161 aa)
panEKetopantoate reductase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the ketopantoate reductase family. (303 aa)
folPDihydropteroate synthase; Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. Belongs to the DHPS family. (285 aa)
coaXPantothenate kinase; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. Cannot utilize a phosphoryl donor other than ATP; Belongs to the type III pantothenate kinase family. (258 aa)
clpPATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] (197 aa)
coaEDephosphocoenzyme A kinase; Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A; Belongs to the CoaE family. (197 aa)
pykPyruvate kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; In the C-terminal section; belongs to the PEP-utilizing enzyme family. (585 aa)
yuxHPutative phosphodiesterase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (409 aa)
tpiATriose phosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family. (253 aa)
panCPantothenate synthetase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Belongs to the pantothenate synthetase family. (286 aa)
dxr1-deoxy-D-xylulose-5-phosphate reductoisomerase; Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4- phosphate (MEP); Belongs to the DXR family. (383 aa)
panE-22-dehydropantoate 2-reductase; Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. (298 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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