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
fabG-23-ketoacyl-ACP reductase; Catalyzes the first of the two reduction steps in the elongation cycle of fatty acid synthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (239 aa)    
Predicted Functional Partners:
fabZ
hydroxymyristoyl-ACP dehydratase; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
     
 0.903
fusB
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.903
AIY10433.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.901
lgrD
Peptide synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.855
fabH-2
3-oxoacyl-ACP synthase; 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.
 
 
 0.812
nrsA
Asparagine adenylase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.754
AIY10565.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.749
fabH5
3-oxoacyl-ACP synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.679
fabH
3-oxoacyl-ACP synthase; 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.
  
 
 0.679
fusC
3-oxoacyl-ACP synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.
 
   
 0.655
Your Current Organism:
Paenibacillus polymyxa
NCBI taxonomy Id: 1406
Other names: ATCC 842, Aerobacillus polymyxa, Bacillus polymyxa, Bacillus sp. NCIM 2538, Bacillus sp. NCIM 2540, Bacillus sp. NCIM 2726, Bacillus sp. RP 2.2, CCUG 7426, CFBP 4258, CIP 66.22, Clostridium polymyxa, DSM 36, Granulobacter polymyxa, HAMBI 635, IAM 13419, IFO 15309, JCM 2507, LMG 13294, LMG:13294, NBRC 15309, NCCB 24016, NCIB 8158, NCIB:8158, NCTC 10343, NRRL B-4317, P. polymyxa, Paenibacillus sp. JCM 8035, Paenibacillus sp. JCM 8036, Paenibacillus sp. JCM 8037, Paenibacillus sp. JCM 8038, Paenibacillus sp. JCM 8039, Paenibacillus sp. WLY78, VKM B-514
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