STRINGSTRING
mmgA mmgA caiD caiD accA accA pccB pccB mutB mutB mutA mutA gabT gabT CBL56582.1 CBL56582.1 lpd lpd ilvE ilvE iolA iolA aldB aldB mmsB mmsB
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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
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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
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
mmgA2 Acetyl-CoA <=> CoA + Acetoacetyl-CoA and Acetyl-CoA + Butanoyl-CoA <=> CoA + 3-Oxohexanoyl-CoA; Belongs to the thiolase-like superfamily. Thiolase family. (384 aa)
caiDEnoyl-CoA hydratase/carnithine racemase CaiD. (310 aa)
accAATP + acetyl-CoA + HCO(3)(-) <=> ADP + phosphate + malonyl-CoA. (593 aa)
pccBPropionyl-CoA carboxylase beta chain; ATP + propanoyl-CoA + HCO(3)(-) <=> ADP + phosphate + (S)-methylmalonyl-CoA. (524 aa)
mutBMethylmalonyl-CoA mutase catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. Induced by heat and acid stresses. (728 aa)
mutAMethylmalonyl-CoA mutase small subunit (Methylmalonyl-CoA mutase beta subunit) (MCB-beta); Methylmalonyl-CoA mutase catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. Induced by heat and acid stresses. (638 aa)
gabT4-aminobutyrate aminotransferase; 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde +; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (445 aa)
CBL56582.1Methylmalonyl-CoA epimerase; (R)-2-Methyl-3-oxopropanoyl-CoA <=> (S)-2-Methyl-3-oxopropanoyl-CoA. (148 aa)
lpdIn the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system, in which it acts with EC 1.4.4.2 and EC 2.1.2.10 to break down glycine. (466 aa)
ilvECatalyzes the first reaction in the catabolism of the branched chain amino acids leucine, isoleucine, and valine. pyridoxal-phosphate dependent enzymes. (361 aa)
iolAiolA (Myo-inositol catabolism IolA protein) (Methylmalonic acid semialdehyde dehydrogenase); * 3-Oxopropanoate + CoA + NAD+ <=> Acetyl-CoA + CO2 + NADH + H+. (501 aa)
aldB(S)-lactaldehyde + NAD(+) + H(2)O <=> (S)-lactate + NADH; Belongs to the aldehyde dehydrogenase family. (498 aa)
mmsB3-hydroxyisobutyrate dehydrogenase related beta-hydroxyacid dehydrogenase. (266 aa)
Your Current Organism:
Propionibacterium freudenreichii
NCBI taxonomy Id: 754252
Other names: P. freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii ATCC 9614, Propionibacterium freudenreichii subsp. shermanii CIP 103027, Propionibacterium freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii str. CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii strain CIRM-BIA1
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