STRINGSTRING
aas aas AEX50918.1 AEX50918.1 fadI fadI fadJ fadJ AEX51347.1 AEX51347.1 AEX51894.1 AEX51894.1 AEX51963.1 AEX51963.1 AEX52010.1 AEX52010.1 AEX52723.1 AEX52723.1 AEX53621.1 AEX53621.1 fadB fadB fadA fadA
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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
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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
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experimentally determined
Predicted Interactions
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gene fusions
gene co-occurrence
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textmining
co-expression
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Your Input:
aasacyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1; In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. (721 aa)
AEX50918.1PFAM: Acyl-CoA dehydrogenase, C-terminal domain; Acyl-CoA dehydrogenase, middle domain; Domain of unknown function (DUF1974); Acyl-CoA dehydrogenase, N-terminal domain. (822 aa)
fadIFatty oxidation complex, beta subunit FadI; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. (437 aa)
fadJFatty oxidation complex, alpha subunit FadJ; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities; In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. (734 aa)
AEX51347.1PFAM: Alcohol dehydrogenase GroES-like domain; Zinc-binding dehydrogenase; TIGRFAM: S-(hydroxymethyl)glutathione dehydrogenase/class III alcohol dehydrogenase; Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily. (374 aa)
AEX51894.1Alcohol dehydrogenase, class IV; PFAM: Aldehyde dehydrogenase family; Iron-containing alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. (889 aa)
AEX51963.1enoyl-CoA hydratase/carnithine racemase; PFAM: Enoyl-CoA hydratase/isomerase family; Belongs to the enoyl-CoA hydratase/isomerase family. (256 aa)
AEX52010.1acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; PFAM: AMP-binding enzyme. (565 aa)
AEX52723.1PFAM: Alcohol dehydrogenase GroES-like domain; Zinc-binding dehydrogenase. (337 aa)
AEX53621.1AMP-forming long-chain acyl-CoA synthetase; PFAM: AMP-binding enzyme. (598 aa)
fadBFatty oxidation complex, alpha subunit FadB; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. (730 aa)
fadAFatty oxidation complex, beta subunit FadA; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. (387 aa)
Your Current Organism:
Rahnella aquatilis
NCBI taxonomy Id: 745277
Other names: R. aquatilis CIP 78.65 = ATCC 33071, Rahnella aquatilis ATCC 33071, Rahnella aquatilis ATCC 33071 = CIP 78.65, Rahnella aquatilis CIP 78.65, Rahnella aquatilis CIP 78.65 = ATCC 33071, Rahnella aquatilis CUETM 77-115, Rahnella aquatilis CUETM 77-155, Rahnella aquatilis DSM 4594
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