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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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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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Toce_03784-hydroxy-2-oxovalerate aldolase; Catalyzes the retro-aldol cleavage of 4-hydroxy-2- oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta- cleavage pathway for the degradation of aromatic compounds. Belongs to the 4-hydroxy-2-oxovalerate aldolase family. (339 aa)    
Predicted Functional Partners:
Toce_0377
Acetaldehyde dehydrogenase; Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds.
 0.999
Toce_0376
COGs: COG3971 2-keto-4-pentenoate hydratase; InterPro IPR002529; KEGG: mta:Moth_1777 4-oxalocrotonate decarboxylase; PFAM: fumarylacetoacetate (FAA) hydrolase; PRIAM: 2-oxopent-4-enoate hydratase; SPTR: 4-oxalocrotonate decarboxylase; PFAM: Fumarylacetoacetate (FAA) hydrolase family; TIGRFAM: 2-oxopent-4-enoate hydratase.
 
 
 0.996
ilvE
Branched chain amino acid aminotransferase apoenzyme; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
  
 
 0.861
Toce_0379
BFD domain protein (2Fe-2S)-binding domain protein; COGs: COG4231 Indolepyruvate ferredoxin oxidoreductase alpha and beta subunits; InterPro IPR017896:IPR017900:IPR007419; KEGG: chy:CHY_1274 iron-sulfur cluster-binding protein; PFAM: BFD domain protein [2Fe-2S]-binding domain protein; SPTR: Iron-sulfur cluster-binding protein; PFAM: 4Fe-4S binding domain; BFD-like [2Fe-2S] binding domain.
 
     0.824
Toce_0380
KEGG: mta:Moth_1773 hypothetical protein; SPTR: Putative uncharacterized protein.
       0.787
Toce_0375
InterPro IPR001453; KEGG: mta:Moth_1778 molybdopterin binding domain-containing protein; PFAM: molybdopterin binding domain; SPTR: Molybdopterin binding domain; PFAM: Probable molybdopterin binding domain; TIGRFAM: molybdenum cofactor synthesis domain.
 
     0.783
Toce_0848
D-amino acid aminotransferase; Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction.
  
 
 0.774
Toce_0374
Quinolinate phosphoribosyl transferase; COGs: COG0157 Nicotinate-nucleotide pyrophosphorylase; InterPro IPR002638; KEGG: mta:Moth_1779 nicotinate-nucleotide pyrophosphorylase; PFAM: Quinolinate phosphoribosyl transferase; SPTR: Nicotinate-nucleotide pyrophosphorylase (Carboxylating); PFAM: Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl transferase, N-terminal domain.
  
  
 0.743
Toce_1803
L-threonine ammonia-lyase; COGs: COG1171 Threonine dehydratase; InterPro IPR005789:IPR001926:IPR002912:IPR000634; KEGG: chy:CHY_2459 threonine dehydratase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; amino acid-binding ACT domain protein; SPTR: Threonine dehydratase; TIGRFAM: threonine dehydratase; PFAM: ACT domain; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine ammonia-lyase, biosynthetic, long form; threonine dehydratase, medium form.
  
  
 0.711
Toce_0381
Benzoate transporter; COGs: COG3135 Uncharacterized protein involved in benzoate metabolism; InterPro IPR003016:IPR004711; KEGG: mta:Moth_1772 benzoate transporter; PFAM: Benzoate membrane transport protein; SPTR: Benzoate transporter; TIGRFAM: benzoate transporter; PFAM: Benzoate membrane transport protein; TIGRFAM: benzoate transporter.
 
     0.701
Your Current Organism:
Thermosediminibacter oceani
NCBI taxonomy Id: 555079
Other names: T. oceani DSM 16646, Thermosediminibacter oceani DSM 16646, Thermosediminibacter oceani JW/IW-1228P, Thermosediminibacter oceani str. DSM 16646, Thermosediminibacter oceani strain DSM 16646
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