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fadE fadE frmA frmA adhE adhE paaF paaF adhP adhP fadD fadD atoB atoB fadJ fadJ fadI fadI hcaD hcaD aas aas yqeF yqeF yiaY yiaY fadA fadA fadB fadB
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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
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second shell of interactors
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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fadEAcyl coenzyme A dehydrogenase; Catalyzes the dehydrogenation of acyl-coenzymes A (acyl-CoAs) to 2-enoyl-CoAs, the first step of the beta-oxidation cycle of fatty acid degradation. Is required for E.coli to utilize dodecanoate or oleate as the sole carbon and energy source for growth. (814 aa)
frmAAlcohol dehydrogenase class III; Has high formaldehyde dehydrogenase activity in the presence of glutathione and catalyzes the oxidation of normal alcohols in a reaction that is not GSH-dependent. In addition, hemithiolacetals other than those formed from GSH, including omega-thiol fatty acids, also are substrates; Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily. (369 aa)
adhEAcetaldehyde dehydrogenase [acetylating]; This enzyme has three activities: ADH, ACDH, and PFL- deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction; In the N-terminal section; belongs to the aldehyde dehydrogenase family. (891 aa)
paaF2,3-dehydroadipyl-CoA hydratase; Catalyzes the reversible conversion of enzymatically produced 2,3-dehydroadipyl-CoA into 3-hydroxyadipyl-CoA. Belongs to the enoyl-CoA hydratase/isomerase family. (255 aa)
adhPEthanol-active dehydrogenase/acetaldehyde-active reductase; Preferred specificity is towards 1-propanol; Belongs to the zinc-containing alcohol dehydrogenase family. (336 aa)
fadDacyl-CoA synthetase (long-chain-fatty-acid--CoA ligase); Catalyzes the esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Activity is the highest with fatty acid substrates of > 10 carbon atoms. Is involved in the aerobic beta- oxidative degradation of fatty acids, which allows aerobic growth of E.coli on fatty acids as a sole carbon and energy source. (561 aa)
atoBacetyl-CoA acetyltransferase; Protein involved in fatty acid oxidation. (394 aa)
fadJenoyl-CoA hydratase/epimerase and isomerase/3-hydroxyacyl-CoA dehydrogenase; 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. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids; In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. (714 aa)
fadIbeta-ketoacyl-CoA thiolase, anaerobic, subunit; 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. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids. Belongs to the thiolase-like superfamily. Thiolase family. (436 aa)
hcaDPhenylpropionate dioxygenase, ferredoxin reductase subunit; Part of the multicomponent 3-phenylpropionate dioxygenase, that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid- dihydrodiol (CI-dihydrodiol), respectively; Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin reductase family. (400 aa)
aasFused 2-acylglycerophospho-ethanolamine acyl transferase/acyl-acyl carrier protein synthetase; 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. (719 aa)
yqeFShort chain acyltransferase; Putative acyltransferase; Belongs to the thiolase-like superfamily. Thiolase family. (393 aa)
yiaYL-threonine dehydrogenase; Putative oxidoreductase. (383 aa)
fadA3-ketoacyl-CoA thiolase (thiolase I); 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. Involved in the aerobic and anaerobic degradation of long-chain fatty acids. (387 aa)
fadBEnoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase; 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 C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. (729 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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