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
AEB84223.1PFAM: Short-chain dehydrogenase/reductase SDR; KEGG: eba:ebA5300 putative dehydrogenase; SMART: Polyketide synthase/Fatty acid synthase, KR. (252 aa)    
Predicted Functional Partners:
AEB83669.1
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.
 
 0.951
AEB83001.1
PFAM: Beta-ketoacyl synthase, N-terminal; Beta-ketoacyl synthase, C-terminal; KEGG: dia:Dtpsy_0542 beta-ketoacyl synthase; SMART: Polyketide synthase, beta-ketoacyl synthase domain; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
 
 0.947
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.
 
 0.938
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.
 
 
 0.935
AEB83002.1
Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabA; Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E- (2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length.
  
 0.929
AEB83906.1
3-alpha,7-alpha, 12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoAhydratase; KEGG: bpa:BPP0606 putative enoyl-CoA hydratase; PFAM: MaoC-like dehydratase.
 
 0.927
AEB84230.1
3-alpha,7-alpha, 12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoAhydratase; KEGG: pol:Bpro_5282 MaoC-like dehydratase; PFAM: MaoC-like dehydratase.
 
 0.806
AEB86223.1
KEGG: app:CAP2UW1_1324 oxidoreductase FAD-binding domain protein; PFAM: Oxidoreductase, FAD-binding domain; Ferredoxin; Cytochrome b/b6, N-terminal; Oxidoreductase FAD/NAD(P)-binding.
 
 0.768
AEB82592.1
3-alpha,7-alpha, 12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoAhydratase; KEGG: ajs:Ajs_0121 dehydratase; PFAM: MaoC-like dehydratase.
 
 0.744
AEB82580.1
3-alpha,7-alpha, 12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoAhydratase; KEGG: reh:H16_A2151 putative acyl dehydratase; PFAM: MaoC-like dehydratase.
 
 0.701
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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