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sdaAB sdaAB serA serA mleA mleA rsh rsh pheA pheA yszB yszB dapG dapG purU purU yclM yclM tyrA tyrA hom hom lysC lysC ilvH ilvH
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
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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
Others
textmining
co-expression
protein homology
Your Input:
sdaABL-serine dehydratase (beta chain); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. (220 aa)
serA3-phosphoglycerate dehydrogenase; Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L- serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate. (525 aa)
mleANAD-dependent malic enzyme (conversion of malate into pyruvate); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (439 aa)
rshGTP pyrophosphokinase (RelA/SpoT); In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp, it is probably the hydrolysis activity that is required for optimal growth (Probable); Belongs to the RelA/SpoT family. (734 aa)
pheAPrephenate dehydratase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (285 aa)
yszBConserved hypothetical protein containing an ACT domain; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 2537815; Belongs to the UPF0735 family. (147 aa)
dapGAspartokinase I (alpha and beta subunits); Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine. Belongs to the aspartokinase family. (404 aa)
purUFormyltetrahydrofolate hydrolase; Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4). (300 aa)
yclMAspartate kinase III; Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine. (454 aa)
tyrAPrephenate dehydrogenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the prephenate/arogenate dehydrogenase family. (371 aa)
homHomoserine dehydrogenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (433 aa)
lysCAspartokinase II alpha subunit (aa 1->408) and beta subunit (aa 246->408); Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine. (408 aa)
ilvHAcetolactate synthase (acetohydroxy-acid synthase) (small subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the acetolactate synthase small subunit family. (172 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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