STRINGSTRING
STRING protein interaction network
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.
Node Color
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
Edges:
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
icdAIsocitrate dehydrogenase NADP-dependent, monomeric type; NADP(+)-dependent isocitrate dehydrogenase (ICD) is an important enzyme of the intermediary metabolism, as it controls the carbon flux within the citric acid cycle and supplies the cell to 2-oxoglutarate and NADPH for biosynthetic purposes; The activity of this enzyme, which is controlled by phosphorylation, helps regulate carbon flux between the Krebs cycle and the glyoxylate bypass, which is an alternate route that accumulates carbon for biosynthesis when acetate is the sole carbon source for growth; Localized in the cytoplasm; [...] (739 aa)    
Predicted Functional Partners:
acnA
Aconitate hydratase is involved in the tricarboxylic acid cycle. It catalyzes the reversible, stereo-specific, isomerization of citrate to isocitrate via cis-aconitate. It displays a N-terminal catalytic domain which binds a 4Fe-4S cluster and a C-terminal domain which undergoes conformational change in the enzyme mechanism; Localized in the cytoplasm; High confidence in function and specificity.
 
 
 0.980
aatB
Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity.
 
 
 
  0.920
sucA
The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3); High confidence in function and specificity.
   
 
 0.918
mdh
Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate.
  
  
 0.878
gltA-2
Glutamate synthase [NADPH] large chain; Glutamate synthase is a key enzyme in the early stages of the assimilation of ammonia. It is a complex iron-sulfur flavoprotein catalyzing the reductive transfer of the amido nitrogen from L-glutamine to 2-oxoglutarate to form two molecules of L-glutamate via intramolecular channelling of ammonia from the amidotransferase domain to the FMN-binding domain. Glutamate synthase forms an aggregate of 4 catalytic active heterodimers, consisting of a large and a small subunit (GltB). GltA binds as cofactors a 3Fe-4S cluster, a FAD and a FMN. Localized i [...]
     
 0.865
purB
Adenylosuccinate lyase catalyzes step 8 in the pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP. It cleaves succinylaminoimidazole carboxamide ribotide into aminoimidazole carboxamide ribotide and fumarate, as well as adenylosuccinate into adenylate and fumarate. Localized in the cytoplasm; High confidence in function and specificity.
   
  0.826
argH
Argininosuccinate lyase is involved in the eighth and last step of the arginine biosynthesis pathway. It converts the Omega-N-(L-arginino)succinate to fumarate and L-arginine; Belongs to the fumarate lyase family. Localized in the cytoplasm; High confidence in function and specificity.
    
 0.815
gdhA1
Glutamate dehydrogenase catalyzes the NAD- and/or NADP-dependent reversible deamination of L-glutamate into alpha-ketoglutarate. It is involved with either ammonia assimilation or glutamate catabolism. Forms a homohexamer and binds one NAD(P) cofactor by subunit. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
   
 
 0.813
gdhA2
Glutamate dehydrogenase catalyzes the NAD- and/or NADP-dependent reversible deamination of L-glutamate into alpha-ketoglutarate. It is involved with either ammonia assimilation or glutamate catabolism. Forms a homohexamer and binds one NAD(P) cofactor by subunit. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
   
 
 0.813
gltB
Glutamate synthase [NADPH] small chain; Glutamate synthase is a key enzyme in the early stages of the assimilation of ammonia. It is a complex iron-sulfur flavoprotein catalyzing the reductive transfer of the amido nitrogen from L-glutamine to 2-oxoglutarate to form two molecules of L-glutamate via intramolecular channelling of ammonia from the amidotransferase domain to the FMN-binding domain. Glutamate synthase forms an aggregate of 4 catalytic active heterodimers, consisting of a large (GltA) and a small subunit. GltB binds NADP(H) as a cofactor. Localized in the cytoplasm; High con [...]
   
 
 0.810
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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