STRINGSTRING
cypA cypA cypC cypC cypD cypD yjiB yjiB pksS pksS cypB cypB bioI bioI cypX cypX
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.
Node Color
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
cypACytochrome P450; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (410 aa)
cypCFatty acid beta-hydroxylating cytochrome P450; Catalyzes the alpha- and beta-hydroxylation of myristic acid in the presence of hydrogen peroxide; Belongs to the cytochrome P450 family. (417 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)
yjiBPutative monooxygenase (cytochrome P450); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (396 aa)
pksSCytochrome P450 of bacillaene metabolism; Involved in the metabolism of the antibiotic polyketide bacillaene which is involved in secondary metabolism. The substrate is dihydrobacillaene. (405 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)
bioICytochrome P450 for pimelic acid formation for biotin biosynthesis; Catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. It has high affinity for long-chain fatty acids with the greatest affinity for myristic acid; Belongs to the cytochrome P450 family. (395 aa)
cypXcyclo-L-leucyl-L-leucyl dipeptide oxidase; Involved in the biosynthesis of pulcherrimin, a red extracellular pigment. Catalyzes the oxidation of cyclo(L-Leu-L-Leu) (cLL) to yield pulcherriminic acid which forms pulcherrimin via a nonenzymic reaction with Fe(3+). Substrates with small alkyl groups (cAA, cLG, cLP) exhibit weaker binding to CYP134A1, but substrates with larger hydrophobic side chains bind in a similar regime to cLL. Belongs to the cytochrome P450 family. (405 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
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.