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
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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.
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
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Score
ADO46521.12,4-diaminobutyrate 4-transaminase; KEGG: pct:PC1_2060 diaminobutyrate--2-oxoglutarate aminotransferase; TIGRFAM: 2,4-diaminobutyrate 4-transaminase; PFAM: aminotransferase class-III; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (460 aa)    
Predicted Functional Partners:
ADO46520.1
PFAM: Pyridoxal-dependent decarboxylase; KEGG: ebi:EbC_22090 L-2,4-diaminobutyrate decarboxylase.
 0.994
ADO49957.1
Aspartate kinase; KEGG: kpu:KP1_0820 bifunctional aspartokinase I/homeserine dehydrogenase I; TIGRFAM: aspartate kinase; PFAM: homoserine dehydrogenase; aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; homoserine dehydrogenase NAD-binding; In the C-terminal section; belongs to the homoserine dehydrogenase family.
    
 0.940
ADO50564.1
Aspartate kinase; KEGG: cko:CKO_03054 bifunctional aspartate kinase II/homoserine dehydrogenase II; TIGRFAM: aspartate kinase; PFAM: homoserine dehydrogenase; aspartate/glutamate/uridylate kinase; homoserine dehydrogenase NAD-binding; In the C-terminal section; belongs to the homoserine dehydrogenase family.
    
 0.940
asd
Aspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family.
    
 0.923
ADO50375.1
TIGRFAM: aspartate kinase; aspartate kinase, monofunctional class; KEGG: cko:CKO_03894 aspartate kinase III; PFAM: aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; Belongs to the aspartokinase family.
    
 0.793
ADO49454.1
Amino acid adenylation domain protein; KEGG: kpe:KPK_3973 enterobactin synthase subunit F; TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; phosphopantetheine-binding; Thioesterase.
  
  
 0.644
ADO47148.1
KEGG: cko:CKO_04008 succinate-semialdehyde dehydrogenase I; TIGRFAM: succinic semialdehyde dehydrogenase; PFAM: Aldehyde Dehydrogenase; Belongs to the aldehyde dehydrogenase family.
  
 
 0.627
ADO48486.1
PFAM: Aldehyde Dehydrogenase; KEGG: kpu:KP1_2509 aldehyde dehydrogenase A; Belongs to the aldehyde dehydrogenase family.
  
 
 0.627
ADO49058.1
KEGG: kva:Kvar_3367 succinic semialdehyde dehydrogenase; TIGRFAM: succinic semialdehyde dehydrogenase; PFAM: Aldehyde Dehydrogenase; Belongs to the aldehyde dehydrogenase family.
  
 
 0.627
lhgD
FAD dependent oxidoreductase; Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG) to alpha-ketoglutarate and couples to the respiratory chain by feeding electrons from the reaction into the membrane quinone pool. Functions in a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. Reaction=(S)-2-hydroxyglutarate + a quinone = 2-oxoglutarate + a quinol; Xref=Rhea:RHEA:58664, ChEBI:CHEBI:16782, ChEBI:CHEBI:16810, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58665; Belongs to the L2HGDH family.
  
  
 0.616
Your Current Organism:
Enterobacter lignolyticus
NCBI taxonomy Id: 701347
Other names: Enterobacter lignolyticus SCF1, [. lignolyticus SCF1, [Enterobacter] lignolyticus SCF1
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