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psd psd panD panD ulaD ulaD ldcC ldcC speF speF trpC trpC pyrF pyrF gadB gadB oxc oxc lysA lysA speA speA speC speC pck pck gadA gadA sgbH sgbH dfp dfp ubiD ubiD hemE hemE adiA adiA cadA cadA speD speD
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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psdPhosphatidylserine decarboxylase; Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Only decarboxylates the lipid-linked form of the serine moiety, and not serine alone or derivatives like phosphoserine or glycerophosphoserine. (322 aa)
panDAspartate 1-decarboxylase; Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine; Belongs to the PanD family. (126 aa)
ulaD3-keto-L-gulonate 6-phosphate decarboxylase; Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. Is involved in the anaerobic L-ascorbate utilization. Belongs to the HPS/KGPDC family. KGPDC subfamily. (216 aa)
ldcCLysine decarboxylase 2, constitutive; Plays a role in lysine utilization by acting as a lysine decarboxylase. (713 aa)
speFOrnithine decarboxylase isozyme, inducible; Protein involved in polyamine biosynthetic process; Belongs to the Orn/Lys/Arg decarboxylase class-I family. (732 aa)
trpCIndole-3-glycerolphosphate synthetase and N-(5-phosphoribosyl)anthranilate isomerase; Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain. (453 aa)
pyrFOrotidine-5'-phosphate decarboxylase; Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). (245 aa)
gadBGlutamate decarboxylase B, PLP-dependent; Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria; Belongs to the group II decarboxylase family. (466 aa)
oxcOxalyl CoA decarboxylase, ThDP-dependent; Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Catalyzes the decarboxylation of oxalyl-CoA to yield carbon dioxide and formyl-CoA; Belongs to the TPP enzyme family. (564 aa)
lysADiaminopimelate decarboxylase, PLP-binding; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine. Is not active against the DD- or LL-isomers of diaminopimelate; Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily. (420 aa)
speABiosynthetic arginine decarboxylase, PLP-binding; Catalyzes the biosynthesis of agmatine from arginine. Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily. (658 aa)
speCOrnithine decarboxylase, constitutive; Ornithine decarboxylase isozyme; Protein involved in polyamine biosynthetic process. (711 aa)
pckPhosphoenolpyruvate carboxykinase [ATP]; Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA. Belongs to the phosphoenolpyruvate carboxykinase (ATP) family. (540 aa)
gadAGlutamate decarboxylase A, PLP-dependent; Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria. (466 aa)
sgbH3-keto-L-gulonate 6-phosphate decarboxylase; Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. May be involved in the utilization of 2,3-diketo-L- gulonate. (220 aa)
dfpCoenzyme 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)
ubiD3-octaprenyl-4-hydroxybenzoate decarboxylase; Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis; Belongs to the UbiD family. (497 aa)
hemEUroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. (354 aa)
adiAArginine decarboxylase; ADC can be found in two forms: biodegradative and biosynthetic. The biodegradative form may play a role in regulating pH by consuming proteins; Belongs to the Orn/Lys/Arg decarboxylase class-I family. (755 aa)
cadALysine decarboxylase, acid-inducible; Inducible lysine decarboxylase that catalyzes the proton- dependent decarboxylation of L-lysine to produce the polyamine cadaverine and carbon dioxide. Plays a role in pH homeostasis by consuming protons and neutralizing the acidic by- products of carbohydrate fermentation. Belongs to the Orn/Lys/Arg decarboxylase class-I family. (715 aa)
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. (264 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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