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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
sucCsuccinyl-CoA synthase, 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. (397 aa)    
Predicted Functional Partners:
sucD
succinyl-CoA synthase, 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
sucD-2
malate--CoA ligase, 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
sdhC
Succinate dehydrogenase, cytochrome b556 subunit; Identified by match to protein family HMM PF01127.
  
 
 0.984
sdhB
Succinate dehydrogenase, iron-sulfur protein; Identified by match to protein family HMM TIGR00384; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
 0.984
sucB
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; 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).
 0.983
sdhD
Succinate dehydrogenase, hydrophobic membrane anchor protein; Identified by similarity to GB:AAC17941.1.
  
 
 0.978
sdhA
Succinate dehydrogenase, flavoprotein subunit; Identified by similarity to SP:P31038; match to protein family HMM PF00890; match to protein family HMM PF02910; match to protein family HMM TIGR01812; match to protein family HMM TIGR01816; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
 0.973
sucA
2-oxoglutarate dehydrogenase, E1 component; Identified by match to protein family HMM PF00676; match to protein family HMM PF02779; match to protein family HMM TIGR00239.
 0.965
SPO1469
3-ketosteroid dehydrogenase, putative; Identified by similarity to GB:AAF19054.1; match to protein family HMM PF00890.
  
 0.952
SPO1105
methylmalonyl-CoA mutase; Identified by similarity to SP:O86028; match to protein family HMM PF01642; match to protein family HMM PF02310; match to protein family HMM TIGR00640; match to protein family HMM TIGR00641.
  
 
 0.933
Your Current Organism:
Ruegeria pomeroyi
NCBI taxonomy Id: 246200
Other names: R. pomeroyi DSS-3, Ruegeria pomeroyi DSS-3, Ruegeria pomeroyi str. DSS-3, Ruegeria pomeroyi strain DSS-3, Silicibacter pomeroyi DSS-3
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