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bsdB bsdB bsdC bsdC bsdD bsdD cypD cypD yfmT yfmT yflL yflL cypB cypB yutF yutF
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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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experimentally determined
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bsdBPhenolic acid decarboxylase subunit BsdB; Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions. Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for phenolic acid decarboxylase (By similarity); Belongs to the UbiX/PAD1 family. YclB subfamily. (204 aa)
bsdCPhenolic acid decarboxylase subunit BsdC; Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions. Phenolic acid decarboxylase that catalyzes the reversible decarboxylation of 4- hydroxybenzoate and vanillate. Could also catalyze the decarboxylation of salicylate (Probable). Is not active on di- and tri-hydroxybenzoate derivatives. Belongs to the UbiD family. YclC subfamily. (473 aa)
bsdDPhenolic acid decarboxylase subunit BsdD; Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions, however the precise biochemical function of BsdD in metabolism of phenolic acid is unknown. (75 aa)
cypDPutative bifunctional P-450/NADPH-P450 reductase 1; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 position. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain. Is also able to catalyze efficient oxidation of sodium dodecyl sulfate (SDS). (1061 aa)
yfmTPutative aldehyde dehydrogenase; A benzaldehyde dehydrogenase able to act on substrates with 3- and 4-hydroxy and methoxy substitutions; converts vanillin (4- hydroxy-3-methoxybenzaldehyde) to vanillic acid in vitro. The physiological substrate is unknown. (485 aa)
yflLPutative acylphosphatase; 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 acylphosphatase family. (91 aa)
cypBCytochrome P450 CYP102A3; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain. (1054 aa)
yutFPutative p-nitrophenyl phosphatase; Catalyzes the dephosphorylation of 2-6 carbon acid sugars in vitro; Belongs to the HAD-like hydrolase superfamily. NagD family. (256 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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