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speD speD speE speE proC proC codA codA proA proA proB proB speF speF astC astC astA astA astD astD astB astB astE astE speG speG puuA puuA puuD puuD puuC puuC puuB puuB putA putA aspC aspC speB speB speA speA speC speC ygjG ygjG adiA adiA
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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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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
protein homology
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speDS-adenosylmethionine decarboxylase; 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 2 subfamily. (264 aa)
speESpermidine synthase (putrescine aminopropyltransferase); Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. (288 aa)
proCPyrroline-5-carboxylate reductase, NAD(P)-binding; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. (269 aa)
codACytosine deaminase; Function experimentally demonstrated in the studied species; enzyme. (427 aa)
proAGamma-glutamylphosphate 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. (417 aa)
proBGamma-glutamate kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. (367 aa)
speFOrnithine decarboxylase isozyme, inducible; Function experimentally demonstrated in the studied species; enzyme. (732 aa)
astCSuccinylornithine transaminase, PLP-dependent; Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily. (406 aa)
astAArginine succinyltransferase; Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. (344 aa)
astDSuccinylglutamic semialdehyde dehydrogenase; Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate. (492 aa)
astBSuccinylarginine dihydrolase; Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)- succinylornithine, ammonia and CO(2). (447 aa)
astESuccinylglutamate desuccinylase; Transforms N(2)-succinylglutamate into succinate and glutamate; Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily. (322 aa)
speGSpermidine N1-acetyltransferase; Function experimentally demonstrated in the studied species; enzyme. (186 aa)
puuAgamma-Glu-putrescine synthase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the glutamine synthetase family. (472 aa)
puuDgamma-Glu-GABA hydrolase; Function experimentally demonstrated in the studied species; enzyme. (254 aa)
puuCgamma-Glu-gamma-aminobutyraldehyde dehydrogenase, NAD(P)H-dependent; Function experimentally demonstrated in the studied species; enzyme; Belongs to the aldehyde dehydrogenase family. (495 aa)
puuBgamma-Glu-putrescine oxidase, FAD/NAD(P)-binding; Function experimentally demonstrated in the studied species; enzyme. (426 aa)
putAFused DNA-binding transcriptional regulator; Oxidizes proline to glutamate for use as a carbon and nitrogen source; Belongs to the aldehyde dehydrogenase family. In the N-terminal section; belongs to the proline dehydrogenase family. (1320 aa)
aspCAspartate aminotransferase, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme. (396 aa)
speBAgmatinase; Catalyzes the formation of putrescine from agmatine. Belongs to the arginase family. Agmatinase subfamily. (306 aa)
speABiosynthetic arginine decarboxylase, PLP-binding; Catalyzes the biosynthesis of agmatine from arginine. (658 aa)
speCOrnithine decarboxylase, constitutive; Function experimentally demonstrated in the studied species; enzyme. (711 aa)
ygjGPutrescine:2-oxoglutaric acid aminotransferase, PLP-dependent; Catalyzes the aminotransferase reaction from putrescine to 2- oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline. This is the first step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate (gamma-aminobutyrate or GABA) via 4- aminobutanal. Also functions as a cadaverine transaminase in a a L- lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. (468 aa)
adiABiodegradative arginine decarboxylase; Function experimentally demonstrated in the studied species; enzyme. (756 aa)
Your Current Organism:
Escherichia coli IAI39
NCBI taxonomy Id: 585057
Other names: E. coli IAI39
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