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cypD cypD yflL yflL dhaS dhaS adhB adhB adhA adhA ackA ackA ytcI ytcI acsA acsA pta pta ywdH ywdH aldY aldY aldX aldX glxK glxK
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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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Known Interactions
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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)
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)
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)
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)
adhAPutative dehydrogenase; Functions in the protection against aldehyde-stress. Belongs to the zinc-containing alcohol dehydrogenase family. (349 aa)
ackAAcetate kinase; Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. Appears to favor the formation of acetate. Involved in the secretion of excess carbohydrate. (395 aa)
ytcIPutative acyl-coenzyme A synthetase; 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 ATP-dependent AMP-binding enzyme family. (529 aa)
acsAacetyl-CoA synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA (By similarity). Has a role in growth and sporulation on acetate. (572 aa)
ptaPhosphotransacetylase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (323 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)
glxKGlycerate kinase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (382 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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