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
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[Homology]
Score
fabG3-oxoacyl-ACP 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. (242 aa)    
Predicted Functional Partners:
nuoC
NADH-quinone oxidoreductase subunit 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.
   
 
 0.999
fabD
Malonyl CoA-acyl carrier protein transacylase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.997
fabF
Beta-ketoacyl-[acyl-carrier-protein] synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.
 
 0.986
fabB
FabB, beta-Ketoacyl-ACP synthase I, KASI; catalyzes a condensation reaction in fatty acid biosynthesis: addition of an acyl acceptor of two carbons from malonyl-ACP; required for the elongation of short-chain unsaturated acyl-ACP; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
  
 0.986
fabZ
3-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.
  
 0.975
fabI
Enoyl-[acyl-carrier-protein] reductase; Catalyzes a key regulatory step in fatty acid biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
0.921
fabG_1
3-oxoacyl-ACP reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 
0.914
fadB
Multifunctional fatty acid oxidation complex subunit alpha; 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 N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
  
 0.798
acpP
Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis.
 
 
 0.798
gcvP
Glycine dehydrogenase (aminomethyl-transferring); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.
  
 
 0.708
Your Current Organism:
Moraxella lacunata
NCBI taxonomy Id: 477
Other names: ATCC 17967, Bacillus lacunatus, CCUG 4441, CIP A182, DSM 18052, Diplobacille de la conjonctivite subaigue, Diplobacillus moraxenfeld, JCM 20914, LMG 5301, LMG:5301, M. lacunata, NBRC 102154, NCTC 11011, strain Morax 260
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