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.
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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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
fabDMalonyl CoA-acyl carrier protein transacylase; Identified by similarity to SP:P25715; match to protein family HMM PF00698; match to protein family HMM TIGR00128. (318 aa)    
Predicted Functional Partners:
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.
 0.999
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.
 0.999
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.
 
 0.999
fabB
3-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.
 0.999
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.
 0.998
acpP
Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family.
 0.996
fabI
Enoyl-(acyl-carrier-protein) reductase; Identified by similarity to SP:P29132; match to protein family HMM PF00106.
 
 
 0.991
accD
acetyl-CoA carboxylase, carboxyl transferase, beta subunit; Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA; Belongs to the AccD/PCCB family.
 
 
 0.986
accA
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
 
 
 0.973
MCA0927
Putative 3-oxoacyl-(acyl-carrier-protein) reductase; Identified by similarity to SP:P51831; match to protein family HMM PF00106.
 0.971
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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