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
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yafHPutative acyl-CoA dehydrogenase; Acyl-coenzyme A dehydrogenase (ACDH), Protein of unknown function DUF1974, Domain of unknown function (DUF1974). (814 aa)    
Predicted Functional Partners:
fadJ
Fatty acid oxidation complex subunit alpha; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
 
 0.998
fadB
Fatty acid oxidation complex subunit alpha FadB; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
 
 0.997
nuoCD
NADH dehydrogenase I chain C/D; 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.
   
 0.990
fadI
Fatty acid oxidation complex subunit beta; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed.
 
 0.985
fadA
Small (beta) subunit of the fatty acid-oxidizing multienzyme complex; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed.
 
 0.977
vraB
3-ketoacyl-CoA thiolase (Fatty acid oxidation complex beta subunit) (Beta-ketothiolase) (Acetyl-CoA acyltransferase), Thiolase, Thiolase, N-terminal domain, AcCoA-C-Actrans: acetyl-CoA acetyltransferases; Belongs to the thiolase-like superfamily. Thiolase family.
 
 0.973
fabV
Putative short-chain alcohol dehydrogenase; Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon- carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP); Belongs to the TER reductase family.
    
 0.914
ech1
Naphthoate synthase (Dihydroxynaphthoic acid synthetase) (DHNA synthetase), Crotonase, core, Enoyl-CoA hydratase/isomerase family, PaaB1: phenylacetate degradation probable enoyl-CoA hydratase paaB.
  
 0.764
fadD1
Long-chain-fatty-acid-CoA ligase (Long-chain acyl-CoA synthetase).
 
 
 0.684
nuoI
NADH dehydrogenase I chain I; 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.
  
 0.605
Your Current Organism:
Erwinia amylovora
NCBI taxonomy Id: 665029
Other names: E. amylovora CFBP1430, Erwinia amylovora CFBP1430, Erwinia amylovora str. CFBP1430, Erwinia amylovora strain CFBP1430
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