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fadJ fadJ fadE fadE tesB tesB tesA tesA mdfA mdfA fadR fadR paaF paaF paaG paaG paaH paaH fadK fadK fadD fadD fadL fadL fadA fadA fadB fadB
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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
filled nodes:
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Your Input:
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)
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)
tesBacyl-CoA thioesterase 2; Can hydrolyze a broad range of acyl-CoA thioesters. Its physiological function is not known; Belongs to the C/M/P thioester hydrolase family. (286 aa)
tesAacyl-CoA thioesterase 1 and protease I and lysophospholipase L1; TesA is a multifunctional esterase that can act as a thioesterase, lysophospholipase and protease. TesA functions as a thioesterase specific for fatty acyl thioesters of greater than ten carbons, with highest activity on palmitoyl-CoA, cis-vaccenyl-CoA and palmitoleoyl-CoA. TesA also possesses an arylesterase activity towards short acyl-chain aromatic esters such as alpha-naphthyl acetate, alpha-naphthyl butyrate, benzyl acetate and phenyl acetate. Also able to hydrolyze short acyl-chain triacylglycerols such as triacetin [...] (208 aa)
mdfAMultidrug efflux system protein; Efflux pump driven by the proton motive force. Confers resistance to a broad spectrum of chemically unrelated drugs. Confers resistance to a diverse group of cationic or zwitterionic lipophilic compounds such as ethidium bromide, tetraphenylphosphonium, rhodamine, daunomycin, benzalkonium, rifampicin, tetracycline, puromycin, and to chemically unrelated, clinically important antibiotics such as chloramphenicol, erythromycin, and certain aminoglycosides and fluoroquinolones. Overexpression results in isopropyl-beta-D- thiogalactopyranoside (IPTG) exclusi [...] (410 aa)
fadRFatty acid metabolism regulon transcriptional regulator; Multifunctional regulator of fatty acid metabolism. Represses transcription of at least eight genes required for fatty acid transport and beta-oxidation including fadA, fadB, fadD, fadL and fadE. Activates transcription of at least three genes required for unsaturated fatty acid biosynthesis: fabA, fabB and iclR, the gene encoding the transcriptional regulator of the aceBAK operon encoding the glyoxylate shunt enzymes. (239 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)
paaG1,2-epoxyphenylacetyl-CoA isomerase, oxepin-CoA-forming; Catalyzes the reversible conversion of the epoxide to 2- oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA). (262 aa)
paaH3-hydroxyadipyl-CoA dehydrogenase, NAD+-dependent; Catalyzes the oxidation of 3-hydroxyadipyl-CoA to yield 3- oxoadipyl-CoA; Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. (475 aa)
fadKShort chain acyl-CoA synthetase, anaerobic; Catalyzes the esterification, concomitant with transport, of exogenous fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Is maximally active on C6:0, C8:0 and C12:0 fatty acids, while has a low activity on C14-C18 chain length fatty acids. Is involved in the anaerobic beta-oxidative degradation of fatty acids, which allows anaerobic growth of E.coli on fatty acids as a sole carbon and energy source in the presence of nitrate or fumarate as a terminal electron acceptor. Can fun [...] (548 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)
fadLLong-chain fatty acid outer membrane transporter; Involved in translocation of long-chain fatty acids across the outer membrane. It is a receptor for the bacteriophage T2. FadL may form a specific channel; Belongs to the OmpP1/FadL family. (446 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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