STRINGSTRING
acdA acdA yvaB yvaB fadN fadN yngJ yngJ fabF fabF fabHA fabHA plsC plsC fabHB fabHB fadE fadE pucF pucF fadB fadB mmgC mmgC rtbJ rtbJ
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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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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
acdAacyl-CoA dehydrogenase; Involved in the degradation of long-chain fatty acids. (379 aa)
yvaBNADH:dichloroindophenol oxidoreductase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. Confers resistance to catechol, 2- methylhydroquinone (2-MHQ), and diamide. Probably could also reduce benzoquinones produce by the auto-oxidation of catechol and 2- methylhydroquinone. (211 aa)
fadNenoyl-CoA hydratase / 3-hydroxyacyl-CoA dehydrogenase; Involved in the degradation of long-chain fatty acids; Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. (789 aa)
yngJacyl-CoA dehydrogenase, short-chain specific; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the acyl-CoA dehydrogenase family. (380 aa)
fabFBeta-ketoacyl-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. Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. (413 aa)
fabHABeta-ketoacyl-acyl carrier protein synthase III 1; 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. Has some substrate specificity for branched chain acyl-CoA, determining the biosynthesis of branched-chain of fatty acids instead of straight-chain. (312 aa)
plsC1-acylglycerol-phosphate (1-acyl-G3P) acyltransferase; Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) by incorporating an acyl moiety at the 2 position. This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family. (199 aa)
fabHBBeta-ketoacyl-acyl carrier protein synthase III 2; 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. Has some substrate specificity for branched chain acyl-CoA, determining the biosynthesis of branched-chain of fatty acids instead of straight-chain. (325 aa)
fadEacyl-CoA dehydrogenase (FAD dependent); Involved in the degradation of long-chain fatty acids. (594 aa)
pucFAllantoate amidohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S-ureidoglycine, which is unstable and readily undergoes a second deamination by S- ureidoglycine aminohydrolase AllE to yield S-ureidoglycolate and NH3 (By similarity). (412 aa)
fadBenoyl-CoA hydratase; Involved in the degradation of long-chain fatty acids. (258 aa)
mmgCShort chain acyl-CoA dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the acyl-CoA dehydrogenase family. (379 aa)
rtbJAntitoxin of ribonuclease RttI; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. Confers resistance to catechol, 2- methylhydroquinone (2-MHQ), and diamide. Probably could also reduce benzoquinones produce by the auto-oxidation of catechol and 2- methylhydroquinone. (208 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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