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lcfB lcfB yhfS yhfS yhfT yhfT fadH fadH ykuG ykuG yngE yngE yngF yngF yngG yngG yngHA yngHA yngI yngI yngJ yngJ yokU yokU kamA kamA kamB kamB yodQ yodQ yodR yodR yodS yodS yodT yodT mmgF mmgF mmgE mmgE mmgD mmgD mmgC mmgC mmgB mmgB mmgA mmgA etfA etfA etfB etfB fadB fadB fadR fadR lcfA lcfA fadE fadE fadA fadA fadN fadN acdA acdA fadF fadF yxjF yxjF atoB atoB atoA atoA yxjC yxjC
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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
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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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lcfBLong-chain fatty-acid-CoA ligase (degradative); Involved in the degradation of long-chain fatty acids; Belongs to the ATP-dependent AMP-binding enzyme family. (513 aa)
yhfSPutative acetyl-CoA C-acetyltransferase; May be involved in fatty acid metabolism; Belongs to the thiolase-like superfamily. Thiolase family. (364 aa)
yhfTPutative long-chain fatty-acid-CoA ligase; May be involved in fatty acid metabolism; Belongs to the ATP-dependent AMP-binding enzyme family. (479 aa)
fadHPutative 2,4-dienoyl-CoA reductase; Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA (By similarity); Belongs to the short-chain dehydrogenases/reductases (SDR) family. 2,4-dienoyl-CoA reductase subfamily. (254 aa)
ykuGPutative cell wall protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component. (576 aa)
yngEPutative methylcrotonoyl-CoA carboxylase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the AccD/PCCB family. (511 aa)
yngFPutative Methylglutaconyl-CoA hydratase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the enoyl-CoA hydratase/isomerase family. (260 aa)
yngGPutative hydroxymethylglutaryl-CoA lyase; Involved in the catabolism of branched amino acids such as leucine; Belongs to the HMG-CoA lyase family. (299 aa)
yngHABiotin carboxylase/methylcrotonoyl-CoA carboxylase subunit; 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. (444 aa)
yngIPutative acetoacetyl-CoA synthetase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type e: enzyme; Belongs to the ATP-dependent AMP-binding enzyme family. (549 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)
yokUConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (92 aa)
kamALysine 2,3-aminomutase; Catalyzes the interconversion of L-alpha-lysine and L-beta- lysine; Belongs to the radical SAM superfamily. KamA family. (471 aa)
kamBEpsilon-amino-beta-lysine acetyl transferase; In vitro, is able to catalyze the acetylation of beta-lysine to N6-acetyl-beta-lysine, an archaeal osmolyte produced by methanogenic archaea. Its physiological function has not yet been elucidated. (275 aa)
yodQPutative deacylase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (436 aa)
yodRPutative acyloate-acetoacetate CoA-transferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (217 aa)
yodSPutative aminoacyloate CoA-transferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (229 aa)
yodTPutative aminovalerate aminotransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (444 aa)
mmgF2-methylisocitrate lyase; Involved in the methylcitric acid cycle. Catalyzes the cleavage of 2-methylisocitrate to yield pyruvate and succinate. (301 aa)
mmgE2-methylcitrate dehydratase; Involved in both the tricarboxylic acid (TCA) and methylcitric acid cycles. Has both 2-methylcitrate dehydratase and citrate dehydratase activities. Catalyzes the dehydration of 2-methylcitrate (2-MC) to yield 2-methyl-cis-aconitate, and the dehydration of citrate to yield cis-aconitate. Cannot form isocitrate. Uses either (2S,3R)- or (2R,3S)-2-methylcitrate. (472 aa)
mmgD2-methylcitrate synthase/citrate synthase III; Involved in both the tricarboxylic acid (TCA) and methylcitric acid cycles. Has both 2-methylcitrate synthase and citrate synthase activities. Catalyzes the condensation of propionyl-CoA and oxaloacetate to yield 2-methylcitrate (2-MC) and CoA, and the condensation of acetyl-CoA and oxaloacetate to yield citrate and CoA. Has 2.3-fold higher activity as a 2-methylcitrate synthase. Catalyzes the formation of either (2S,3R)- or (2R,3S)-2-methylcitrate. (372 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)
mmgB3-hydroxybutyryl-CoA dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. (287 aa)
mmgADegradative acetoacetyl-CoA thiolase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the thiolase-like superfamily. Thiolase family. (393 aa)
etfAElectron transfer flavoprotein (alpha subunit); The electron transfer flavoprotein serves as a specific electron acceptor for other dehydrogenases. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity). (325 aa)
etfBElectron transfer flavoprotein (beta subunit); The electron transfer flavoprotein serves as a specific electron acceptor for other dehydrogenases. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity). (257 aa)
fadBenoyl-CoA hydratase; Involved in the degradation of long-chain fatty acids. (258 aa)
fadRTranscriptional regulator of fatty acids degradation (TetR/AcrR family); Transcriptional regulator in fatty acid degradation. Represses transcription of genes required for fatty acid transport and beta-oxidation, including acdA, fadA, fadB, fadE, fadF, fadG, fadH, fadM, fadN, lcfA and lcfB. Binding of FadR to DNA is specifically inhibited by long chain fatty acyl-CoA compounds of 14-20 carbon atoms in length. (194 aa)
lcfALong chain acyl-CoA ligase (degradative); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (560 aa)
fadEacyl-CoA dehydrogenase (FAD dependent); Involved in the degradation of long-chain fatty acids. (594 aa)
fadAacetyl-CoA C-acyltransferase; Involved in the degradation of long-chain fatty acids; Belongs to the thiolase-like superfamily. Thiolase family. (391 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)
acdAacyl-CoA dehydrogenase; Involved in the degradation of long-chain fatty acids. (379 aa)
fadFPutative iron-sulphur-binding reductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (705 aa)
yxjFPutative dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (257 aa)
atoBAcetoacetyl CoA-transferase (subunit B); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the 3-oxoacid CoA-transferase subunit B family. (216 aa)
atoAAcetoacetyl CoA-transferase (subunit A); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the 3-oxoacid CoA-transferase subunit A family. (238 aa)
yxjCPutative permease; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. (472 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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