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
fabB3-oxoacyl-(acyl-carrier-protein) synthase I; Identified by similarity to SP:P14926; match to protein family HMM PF00109; match to protein family HMM PF02801; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. (406 aa)    
Predicted Functional Partners:
fabD
Malonyl CoA-acyl carrier protein transacylase; Identified by similarity to SP:P25715; match to protein family HMM PF00698; match to protein family HMM TIGR00128.
 0.999
fabH-1
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.
 
 0.987
fabA
3-hydroxydecanoyl-(acyl-carrier-protein) dehydratase; 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.
 
 
 0.985
fabI
Enoyl-(acyl-carrier-protein) reductase; Identified by similarity to SP:P29132; match to protein family HMM PF00106.
 
 
 0.975
fabG
3-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.
 0.974
MCA0927
Putative 3-oxoacyl-(acyl-carrier-protein) reductase; Identified by similarity to SP:P51831; match to protein family HMM PF00106.
 0.948
MCA0924
Beta-ketoacyl synthase domain protein; Identified by similarity to GP:17427437; match to protein family HMM PF00109; match to protein family HMM PF02801; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
  
  
 
0.922
fabF
3-oxoacyl-(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.
  
  
0.915
bioC
Biotin synthesis protein BioC; Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L- methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
     
  0.900
fabZ
(3R)-hydroxymyristoyl-(acyl-carrier-protein) 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.
 
 
 0.900
Your Current Organism:
Methylococcus capsulatus
NCBI taxonomy Id: 243233
Other names: M. capsulatus str. Bath, Methylococcus capsulatus ATCC 33009, Methylococcus capsulatus Bath, Methylococcus capsulatus MC, Methylococcus capsulatus NCIB 11132, Methylococcus capsulatus str. Bath
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