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pdhB pdhB sucA sucA sucB sucB lpd3 lpd3 acoA acoA bfmBAB bfmBAB pdhC pdhC lpd_1 lpd_1 lipA lipA lipB lipB
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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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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:
pdhBPyruvate dehydrogenase E1 component subunit beta. (729 aa)
sucA2-oxoglutarate dehydrogenase E1 component. (994 aa)
sucBDihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2). (409 aa)
lpd3Dihydrolipoyl dehydrogenase 3. (468 aa)
acoAAcetoin:2,6-dichlorophenolindophenol oxidoreductase subunit alpha; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (340 aa)
bfmBAB2-oxoisovalerate dehydrogenase subunit beta; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. (464 aa)
pdhCDihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (468 aa)
lpd_1Dihydrolipoyl dehydrogenase. (481 aa)
lipALipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. (324 aa)
lipBOctanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. (238 aa)
Your Current Organism:
Martelella mediterranea
NCBI taxonomy Id: 1122214
Other names: M. mediterranea DSM 17316, Martelella mediterranea DSM 17316
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