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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[Homology]
Score
ADD69761.13-oxoacyl-(acyl-carrier-protein) reductase; Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. Belongs to the short-chain dehydrogenases/reductases (SDR) family. (249 aa)    
Predicted Functional Partners:
ADD69760.1
KEGG: pca:Pcar_1437 malonyl CoA-acyl carrier protein transacylase; TIGRFAM: malonyl CoA-acyl carrier protein transacylase; PFAM: Acyl transferase.
 0.998
ADD69763.1
3-oxoacyl-(acyl-carrier-protein) synthase 2; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.
 0.993
fabH
3-oxoacyl-(acyl-carrier-protein) synthase III; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids; Belongs to the thiolase-like superfamily. FabH family.
 
 0.985
fabZ
Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabZ; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
 
 0.978
ADD69654.1
PFAM: short-chain dehydrogenase/reductase SDR; KEGG: dvm:DvMF_2816 short-chain dehydrogenase/reductase SDR.
 
 
0.944
ADD66847.1
PFAM: short-chain dehydrogenase/reductase SDR; KR domain protein; NAD-dependent epimerase/dehydratase; KEGG: reh:H16_B0101 short chain dehydrogenase.
  
  
 
0.920
acpP
Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis.
 
 
 0.794
ADD66932.1
PFAM: Electron transfer flavoprotein alpha subunit; Electron transfer flavoprotein alpha/beta-subunit; 4Fe- 4S ferredoxin iron-sulfur binding domain protein; KEGG: gur:Gura_1212 electron transfer flavoprotein, alpha subunit.
 
 
 0.791
nuoN
Proton-translocating NADH-quinone oxidoreductase, chain N; 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; Belongs to the complex I subunit 2 family.
   
 
 0.729
nuoD
NADH dehydrogenase I, D subunit; 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; Belongs to the complex I 49 kDa subunit family.
   
 
 0.715
Your Current Organism:
Denitrovibrio acetiphilus
NCBI taxonomy Id: 522772
Other names: D. acetiphilus DSM 12809, Denitrovibrio acetiphilus DSM 12809, Denitrovibrio acetiphilus N2460, Denitrovibrio acetiphilus str. DSM 12809, Denitrovibrio acetiphilus strain DSM 12809
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