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
AGA29192.12-oxoacid:ferredoxin oxidoreductase, beta subunit; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP binding domain. (350 aa)    
Predicted Functional Partners:
AGA29193.1
2-oxoacid:acceptor oxidoreductase, alpha subunit; PFAM: domain; Pyruvate ferredoxin/flavodoxin oxidoreductase; TIGRFAM: 2-oxoacid:acceptor oxidoreductase, alpha subunit.
 
 0.999
AGA26135.1
PFAM: lactate/malate dehydrogenase, alpha/beta C-terminal domain; lactate/malate dehydrogenase, NAD binding domain; Belongs to the LDH/MDH superfamily.
  
 
 0.944
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.
  
 
 0.933
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.
  
 
 0.931
AGA28880.1
PFAM: Malic enzyme, NAD binding domain; Malic enzyme, N-terminal domain.
  
  
 0.931
AGA30539.1
Pyruvate, phosphate dikinase; PFAM: PEP-utilising enzyme, mobile domain; PEP-utilising enzyme, TIM barrel domain; Pyruvate phosphate dikinase, PEP/pyruvate binding domain; TIGRFAM: pyruvate, phosphate dikinase; Belongs to the PEP-utilizing enzyme family.
    
 0.928
AGA31402.1
PFAM: Pyruvate kinase, barrel domain; Pyruvate kinase, alpha/beta domain; TIGRFAM: pyruvate kinase; Belongs to the pyruvate kinase family.
  
 0.924
AGA26065.1
acyl-CoA synthetase/AMP-acid ligase; PFAM: Domain of unknown function (DUF3448); AMP-binding enzyme; TIGRFAM: acetoacetyl-CoA synthase.
  
 
 0.922
acsA
acetate--CoA ligase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA; Belongs to the ATP-dependent AMP-binding enzyme family.
  
 
 0.922
AGA26700.1
PFAM: Citrate synthase; TIGRFAM: citrate synthase I (hexameric type); Belongs to the citrate synthase family.
   
 
 0.920
Your Current Organism:
Singulisphaera acidiphila
NCBI taxonomy Id: 886293
Other names: S. acidiphila DSM 18658, Singulisphaera acidiphila DSM 18658, Singulisphaera acidiphila MOB10, Singulisphaera acidiphila str. DSM 18658, Singulisphaera acidiphila strain DSM 18658
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.