STRINGSTRING
fabZ fabZ lpxC lpxC fadM fadM tesB tesB entH entH ybgC ybgC pal pal fabA fabA fabD fabD fabI fabI paaI paaI fabB fabB fadJ fadJ fadB fadB yiiD yiiD
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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
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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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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
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textmining
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Your Input:
fabZ(3R)-hydroxymyristol acyl carrier protein dehydratase; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. (151 aa)
lpxCUDP-3-O-acyl N-acetylglucosamine deacetylase; Catalyzes the hydrolysis of UDP-3-O-myristoyl-N- acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis. (305 aa)
fadMLong-chain acyl-CoA thioesterase III; Long-chain acyl-CoA thioesterase with a preference for 3,5- tetradecadienoyl-CoA. Could be involved in beta-oxidation of fatty acids; Belongs to the 4-hydroxybenzoyl-CoA thioesterase family. (132 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)
entHEnterobactin synthesis proofreading thioesterase; Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules. Displays esterase activity toward a wide range of substrates, including acyl-CoAs and aryl-CoAs. (137 aa)
ybgCacyl-CoA thioester hydrolase; Thioesterase that appears to be involved in phospholipid metabolism. Some specific acyl-ACPs could be physiological substrates. Displays acyl-CoA thioesterase activity on malonyl-CoA in vitro, catalyzing the hydrolysis of the thioester bond. (134 aa)
palPeptidoglycan-associated outer membrane lipoprotein; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. The Tol-Pal system is also required for polar localization of chemoreceptors clusters. (173 aa)
fabABeta-hydroxydecanoyl thioester dehydrase; Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E- (2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. Is inactive in the dehydration of long chain unsaturated beta-hydroxyacyl-ACP. (172 aa)
fabDmalonyl-CoA-[acyl-carrier-protein] transacylase; Belongs to the FabD family. (309 aa)
fabIEnoyl-[acyl-carrier-protein] reductase, NADH-dependent; Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis. (262 aa)
paaIhydroxyphenylacetyl-CoA thioesterase; Thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters. Hydrolyzes 3,4-dihydroxyphenylacetyl-CoA, 3- hydroxyphenylacetyl-CoA and 4-hydroxyphenylacetyl-CoA. Inactive towards 4-hydroxybenzoyl-CoA and 4-hydroxyphenacyl-CoA. Belongs to the thioesterase PaaI family. (140 aa)
fabB3-oxoacyl-[acyl-carrier-protein] synthase I; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. (406 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)
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)
yiiDGNAT family putative N-acetyltransferase; Putative acetyltransferase. (329 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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