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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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fabH_13-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. (316 aa)    
Predicted Functional Partners:
fabD
Malonyl CoA-ACP transacylase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.998
accD
acetyl-CoA carboxylase subunit beta; 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.
 
 
 0.989
accA_2
acetyl-CoA carboxylase subunit alpha; Catalyzes the carboxylation of acetyl-CoA to malonyl-CoA; forms a tetramer composed of two alpha (AccA) and two beta (AccD) subunits; one of the two catalytic subunits that can form the acetyl CoA carboxylase enzyme together with a carrier protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.988
accB
acetyl-CoA carboxylase; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
 
 
 0.987
accC_1
acetyl-CoA carboxylase; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
 
 
 0.985
fabH_2
3-oxoacyl-ACP synthase; FabH; beta-ketoacyl-acyl carrier protein synthase III; catalyzes the condensation of acetyl-CoA with malonyl-ACP to initiate cycles of fatty acid elongation; this condensing enzyme differs from 3-oxoacyl-(acyl carrier protein) synthase I and II in that it utilizes CoA thioesters as primers rather than acyl-ACPs; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
  0.981
gltA
Type II enzyme; in Escherichia coli this enzyme forms a trimer of dimers which is allosterically inhibited by NADH and competitively inhibited by alpha-ketoglutarate; allosteric inhibition is lost when Cys206 is chemically modified which also affects hexamer formation; forms oxaloacetate and acetyl-CoA and water from citrate and coenzyme A; functions in TCA cycle, glyoxylate cycle and respiration; enzyme from Helicobacter pylori is not inhibited by NADH; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the citrate synthase family.
    
 0.977
aceF
E2 component of pyruvate dehydrogenase multienzyme complex; in Escherichia coli AceF contains three N-terminal lipoyl domains; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.976
acpP
Acyl carrier protein; Carries the fatty acid chain in fatty acid biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.884
AKA10358.1
3-oxoacyl-ACP synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.867
Your Current Organism:
Mannheimia haemolytica
NCBI taxonomy Id: 75985
Other names: ATCC 33396, CCUG 12392, CCUG 408, CIP 103426, DSM 10531, M. haemolytica, NCTC 9380, Pasteurella haemolytica, strain J.A. Watt 1266AB
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