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GYO_0036 GYO_0036 GYO_0525 GYO_0525 GYO_0582 GYO_0582 GYO_1029 GYO_1029 GYO_1248 GYO_1248 dat dat proG proG proB proB proA proA GYO_1804 GYO_1804 proJ proJ proH proH GYO_2300 GYO_2300 GYO_2333 GYO_2333 aspB aspB proI proI GYO_2905 GYO_2905 speD speD GYO_3588 GYO_3588 speB speB speE speE pruA pruA GYO_4287 GYO_4287 GYO_4393 GYO_4393 rocF rocF rocD rocD
Nodes:
Network nodes represent proteins
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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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
GYO_0036YaaO. (480 aa)
GYO_0525Proline dehydrogenase. (251 aa)
GYO_0582Hydrolase, alpha/beta fold family, putative. (281 aa)
GYO_1029Nitric oxide synthase; Catalyzes the production of nitric oxide. Belongs to the NOS family. Bacterial NOS oxygenase subfamily. (363 aa)
GYO_1248Putative aspartate aminotransferase. (393 aa)
datD-amino acid aminotransferase; Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. (282 aa)
proGPyrroline-5-carboxylate reductase 3. (272 aa)
proBGlutamate 5-kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. (365 aa)
proAGamma-glutamyl phosphate reductase; Catalyzes the NADPH-dependent reduction of L-glutamate 5- phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. Belongs to the gamma-glutamyl phosphate reductase family. (415 aa)
GYO_1804Arginine decarboxylase. (490 aa)
proJGlutamate 5-kinase 2; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. (371 aa)
proHPyrroline-5-carboxylate reductase 1; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. (271 aa)
GYO_2300Amine oxidase, flavin-containing. (474 aa)
GYO_2333Aldehyde dehydrogenase; Belongs to the aldehyde dehydrogenase family. (495 aa)
aspBAspartate aminotransferase. (393 aa)
proIPyrroline-5-carboxylate reductase 2; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. (278 aa)
GYO_2905Spermine/spermidine acetyltransferase. (152 aa)
speDS-adenosylmethionine decarboxylase proenzyme; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. (126 aa)
GYO_3588Proline dehydrogenase. (302 aa)
speBAgmatinase; Belongs to the arginase family. (290 aa)
speESpermidine synthase; Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. (276 aa)
pruADelta-1-pyrroline-5-carboxylate dehydrogenase, putative; Belongs to the aldehyde dehydrogenase family. (515 aa)
GYO_4287Benzaldehyde dehydrogenase; Belongs to the aldehyde dehydrogenase family. (485 aa)
GYO_4393Putative aldehyde dehydrogenase AldX; Belongs to the aldehyde dehydrogenase family. (445 aa)
rocFArginase; Belongs to the arginase family. (296 aa)
rocDOrnithine aminotransferase; Catalyzes the interconversion of ornithine to glutamate semialdehyde. (401 aa)
Your Current Organism:
Bacillus subtilis spizizenii
NCBI taxonomy Id: 1052585
Other names: B. subtilis subsp. spizizenii TU-B-10, Bacillus subtilis subsp. spizizenii TU-B-10, Bacillus subtilis subsp. spizizenii str. TU-B-10, Bacillus subtilis subsp. spizizenii strain TU-B-10
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