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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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Score
sucDsuccinyl-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. (290 aa)    
Predicted Functional Partners:
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.
 0.999
sucA
TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; KEGG: pat:Patl_1798 succinate dehydrogenase and fumarate reductase iron-sulfur protein.
 0.992
Ping_2254
KEGG: vch:VC2089 succinate dehydrogenase, flavoprotein subunit; TIGRFAM: succinate dehydrogenase, flavoprotein subunit; succinate dehydrogenase or fumarate reductase, flavoprotein subunit; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
 0.992
Ping_2251
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).
 0.991
Ping_2252
KEGG: ppr:PBPRA1048 putative 2-oxoglutarate dehydrogenase, E1 component; TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: dehydrogenase, E1 component; Transketolase, central region.
 0.991
Ping_3279
KEGG: cvi:CV3368 fumarate reductase, subunit B; TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; PFAM: ferredoxin; 4Fe-4S ferredoxin, iron-sulfur binding domain protein.
 
 0.990
Ping_2256
PFAM: succinate dehydrogenase, cytochrome b subunit; KEGG: vfi:VF0819 succinate dehydrogenase cytochrome b556 subunit.
  
 
 0.989
Ping_3278
KEGG: vfi:VF2334 fumarate reductase flavoprotein subunit; TIGRFAM: fumarate reductase, flavoprotein subunit; succinate dehydrogenase or fumarate reductase, flavoprotein subunit; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein; FAD-dependent pyridine nucleotide-disulphide oxidoreductase.
 0.988
Ping_2255
Succinate dehydrogenase subunit D; Membrane-anchoring subunit of succinate dehydrogenase (SDH).
  
 
 0.980
Ping_2780
Dihydrolipoamide dehydrogenase E3 component of 3 enzyme complexes; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
  
 0.959
Your Current Organism:
Psychromonas ingrahamii
NCBI taxonomy Id: 357804
Other names: P. ingrahamii 37, Psychromonas ingrahamii 37, Psychromonas ingrahamii str. 37, Psychromonas ingrahamii strain 37, gas vacuolate str. 37
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.