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
Sps_01628'PFAM: Dehydrogenase E1 component; Transketolase, pyrimidine binding domain'; 'TIGRFAM: 2-oxoglutarate dehydrogenase, E1 component'. (940 aa)    
Predicted Functional Partners:
Sps_01627
2-oxoglutarate dehydrogenase E2 component; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2).
 0.999
Sps_05377
Dihydrolipoamide dehydrogenase; 'PFAM: Pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain'; TIGRFAM: dihydrolipoamide dehydrogenase.
 
 0.996
Sps_05378
Pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 0.987
Sps_00791
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase component; PFAM: 2-oxoacid dehydrogenases acyltransferase (catalytic domain); e3 binding domain; Biotin-requiring enzyme.
 0.985
Sps_00216
PFAM: 2-oxoacid dehydrogenases acyltransferase (catalytic domain).
 
 0.982
nuoC
NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family.
   
 
 0.962
sucC
succinyl-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.
 
 
 0.960
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.
 
 
 0.959
Sps_01632
PFAM: Succinate dehydrogenase/Fumarate reductase transmembrane subunit; 'TIGRFAM: succinate dehydrogenase, cytochrome b556 subunit'.
 
  
 0.949
Sps_00181
'PFAM: Pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain'; 'TIGRFAM: glutathione-disulfide reductase, animal/bacterial'.
  
 0.948
Your Current Organism:
Shewanella psychrophila
NCBI taxonomy Id: 225848
Other names: CGMCC 1.6159, JCM 13876, S. psychrophila, Shewanella psychrophila Xiao et al. 2007 emend. Thorell et al. 2019, Shewanella sp. WP2, strain WP2
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