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cypD cypD lcfB lcfB yhfS yhfS yhfT yhfT dhaS dhaS mmgA mmgA adhB adhB cypB cypB fadB fadB lcfA lcfA fadA fadA fadN fadN ywdH ywdH aldY aldY aldX aldX
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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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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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:
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)
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)
dhaSPutative aldehyde 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 aldehyde dehydrogenase family. (495 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)
adhBPutative oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily. (378 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)
fadBenoyl-CoA hydratase; Involved in the degradation of long-chain fatty acids. (258 aa)
lcfALong chain acyl-CoA ligase (degradative); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (560 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)
ywdHPutative aldehyde dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (456 aa)
aldYPutative aldehyde dehydrogenase; May contribute to protect cells against stress due to ethanol and related compounds; Belongs to the aldehyde dehydrogenase family. (485 aa)
aldXPutative aldehyde 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 aldehyde dehydrogenase family. (445 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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