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
Databases
Textmining
[Homology]
Score
ADZ10622.1PFAM: 4Fe-4S binding domain; KEGG: mfv:Mfer_0036 2-oxoglutarate ferredoxin oxidoreductase, delta subunit. (69 aa)    
Predicted Functional Partners:
ADZ10621.1
KEGG: mmg:MTBMA_c14150 2-oxoglutarate synthase, subunit alpha; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Transketolase, C-terminal.
 
 
 0.996
ADZ10619.1
KEGG: mru:mru_1826 2-oxoglutarate ferredoxin oxidoreductase subunit gamma KorC; PFAM: Pyruvate/ketoisovalerate oxidoreductase, catalytic domain.
 
 
 0.995
ADZ10620.1
KEGG: mth:MTH1034 2-oxoglutarate ferredoxin oxidoreductase subunit beta; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding.
 
 
 0.991
sucC
Succinyl-CoA ligase (ADP-forming) subunit beta; 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.
    
  0.986
ADZ09693.1
KEGG: mmg:MTBMA_c09230 pyruvate flavodoxin/ferredoxin oxidoreductase, subunit alpha; TIGRFAM: 2-oxoacid:acceptor oxidoreductase, alpha subunit; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain.
  
 
 0.935
ADZ10664.1
TIGRFAM: 2-oxoacid:acceptor oxidoreductase, alpha subunit; KEGG: mmg:MTBMA_c09230 pyruvate flavodoxin/ferredoxin oxidoreductase, subunit alpha; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain.
  
 
 0.935
sucD
succinyl-CoA synthetase, 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.
    
 0.928
ADZ09694.1
TIGRFAM: 2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate; KEGG: ppd:Ppro_0548 pyruvate ferredoxin/flavodoxin oxidoreductase, beta subunit; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding.
  
 
 0.924
ADZ10663.1
TIGRFAM: 2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate; KEGG: mmg:MTBMA_c09240 pyruvate flavodoxin/ferredoxin oxidoreductase, subunit beta; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding.
  
 
 0.924
ADZ10270.1
KEGG: mst:Msp_1077 dihydrolipoamide dehydrogenase-related protein; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase.
 
  
 0.918
Your Current Organism:
Methanobacterium lacus
NCBI taxonomy Id: 877455
Other names: DSM 24406, JCM 17760, M. lacus, Methanobacterium lacus Borrel et al. 2012, Methanobacterium sp. 17A1, Methanobacterium sp. AL-21, strain 17A1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.