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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
sucCsuccinyl-CoA synthetase (ADP-forming) beta subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. (386 aa)    
Predicted Functional Partners:
sucD
succinyl-CoA synthetase (ADP-forming) alpha subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
 0.999
Rmag_0962
PFAM: biotin/lipoyl attachment domain-containing protein; catalytic domain of components of various dehydrogenase complexes; E3 binding domain protein; KEGG: ftl:FTL_0310 pyruvate dehydrogenase, E2 component.
  
 0.985
Rmag_1063
PFAM: Citrate synthase; KEGG: tcx:Tcr_0350 2-methylcitrate synthase/citrate synthase II; Belongs to the citrate synthase family.
  
 0.933
Rmag_0538
TIGRFAM: isocitrate lyase; PFAM: isocitrate lyase and phosphorylmutase; KEGG: son:SO1484 isocitrate lyase.
   
 
 0.922
gcvP
Glycine dehydrogenase (decarboxylating) alpha subunit; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.
   
  
 0.911
Rmag_0423
TIGRFAM: isocitrate dehydrogenase, NADP-dependent; PFAM: isocitrate/isopropylmalate dehydrogenase; KEGG: cbu:CBU_1200 isocitrate dehydrogenase, NADP-dependent.
  
 0.905
Rmag_0992
Aconitase; PFAM: aconitate hydratase domain protein; aconitate hydratase 2; KEGG: noc:Noc_2103 aconitate hydratase; Belongs to the aconitase/IPM isomerase family.
  
  
 0.901
Rmag_0088
TIGRFAM: adenylylsulfate reductase, alpha subunit; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein; KEGG: tbd:Tbd_2282 adenylylsulfate reductase, alpha subunit.
  
 
 0.875
accA
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
    
 0.845
leuA
2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily.
   
 0.826
Your Current Organism:
Ruthia magnifica
NCBI taxonomy Id: 413404
Other names: C. Ruthia magnifica str. Cm (Calyptogena magnifica), Candidatus Ruthia magnifica str. Cm (Calyptogena magnifica), Candidatus Ruthia magnifica strain Cm (Calyptogena magnifica), Ruthia magnifica str. Cm (Calyptogena magnifica)
Server load: low (10%) [HD]