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
ADC62886.1TIGRFAM: succinate dehydrogenase, hydrophobic membrane anchor protein; KEGG: tgr:Tgr7_1466 succinate dehydrogenase, hydrophobic membrane anchor protein. (114 aa)    
Predicted Functional Partners:
ADC62887.1
TIGRFAM: succinate dehydrogenase, cytochrome b556 subunit; PFAM: succinate dehydrogenase cytochrome b subunit; KEGG: tmz:Tmz1t_2550 succinate dehydrogenase, cytochrome b556 subunit.
  
 0.999
ADC62585.1
TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; KEGG: tgr:Tgr7_1481 succinate dehydrogenase and fumarate reductase iron-sulfur protein.
  
 0.998
ADC62885.1
TIGRFAM: succinate dehydrogenase or fumarate reductase, flavoprotein subunit; succinate dehydrogenase, flavoprotein subunit; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein; KEGG: tgr:Tgr7_1467 succinate dehydrogenase, flavoprotein subunit; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
  
 0.997
sucC
succinyl-CoA synthetase, 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.
  
 
 0.988
ADC61922.1
Hydro-lyase, Fe-S type, tartrate/fumarate subfamily, alpha subunit; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.
  
 
 0.983
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.
  
 
 0.962
ADC61256.1
KEGG: aeh:Mlg_2609 2-oxoglutarate dehydrogenase E1 component; TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: Transketolase central region; dehydrogenase E1 component; SMART: Transketolase central region.
  
  
 0.883
ADC62060.1
TIGRFAM: adenylylsulfate reductase, alpha subunit; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein; KEGG: tgr:Tgr7_0350 adenylylsulfate reductase.
  
 
 0.866
ADC62021.1
TIGRFAM: precorrin 3B synthase CobZ; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein; KEGG: rpc:RPC_1893 tricarballylate dehydrogenase.
  
 
 0.862
ADC61322.1
PFAM: aminotransferase class I and II; KEGG: mca:MCA2202 aspartate aminotransferase.
     
  0.800
Your Current Organism:
Allochromatium vinosum
NCBI taxonomy Id: 572477
Other names: A. vinosum DSM 180, Allochromatium vinosum DSM 180, Allochromatium vinosum str. DSM 180, Allochromatium vinosum strain DSM 180
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.