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moaD moaD engD engD thrZ thrZ pucE pucE thrS thrS sdhB sdhB rsh rsh thiS thiS
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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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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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Your Input:
moaDMolybdopterin synthase (small subunit); Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin; Belongs to the MoaD family. (77 aa)
engDPutative GTPase with RNA binding site; ATPase that binds to both the 70S ribosome and the 50S ribosomal subunit in a nucleotide-independent manner. Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. YchF/OLA1 subfamily. (366 aa)
thrZthreonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr); Belongs to the class-II aminoacyl-tRNA synthetase family. (638 aa)
pucEXanthine dehydrogenase, iron-sulfur subunit; Oxidizes hypoxanthine and xanthine to uric acid. (173 aa)
thrSthreonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr); Belongs to the class-II aminoacyl-tRNA synthetase family. (643 aa)
sdhBSuccinate dehydrogenase (iron-sulfur protein); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (253 aa)
rshGTP pyrophosphokinase (RelA/SpoT); In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp, it is probably the hydrolysis activity that is required for optimal growth (Probable); Belongs to the RelA/SpoT family. (734 aa)
thiSSulfur carrier for synthesis of hydroxyethylthiazole phosphate; Is the sulfur donor in the synthesis of the thiazole phosphate moiety of thiamine phosphate; Belongs to the sulfur carrier protein ThiS family. (66 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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