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kbl kbl rimI rimI msbB msbB yjdJ yjdJ phnO phnO plsB plsB aceB aceB metA metA glmU glmU CAR20321.1 CAR20321.1 adhE-3 adhE-3 cysE cysE yiaC yiaC ggt ggt yhbS yhbS tdcE tdcE gcp gcp plsC plsC CAR19590.1 CAR19590.1 glcB glcB yqeF yqeF aas aas argA argA fadA fadA rffC rffC ypfI ypfI maeB maeB eutI eutI ypeA ypeA ddg ddg yfcY yfcY fabB fabB pta pta elaA elaA atoB atoB aat aat pflB pflB mdoC mdoC lpxL lpxL rimJ rimJ fabH fabH fabD fabD fabF fabF nhoA nhoA speG speG astA astA lpxM lpxM yedL yedL wcaB wcaB sucB sucB gltA gltA lnt lnt lipB lipB crcA crcA yafP yafP prpC prpC lacA lacA maa maa lpxA lpxA lpxD lpxD dapD dapD aceF aceF
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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
gene fusions
gene co-occurrence
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textmining
co-expression
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kblGlycine C-acetyltransferase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. (398 aa)
rimIAcetylase for 30S ribosomal subunit protein S18; Acetylates the N-terminal alanine of ribosomal protein S18. (148 aa)
msbBFragment of transposase ORF A, IS600 (partial); Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)- lipid A. (314 aa)
yjdJPutative acyltransferase with acyl-CoA N-acyltransferase domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (90 aa)
phnOPutative acyltransferase with acyl-CoA N-acyltransferase domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (144 aa)
plsBGlycerol-3-phosphate O-acyltransferase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the GPAT/DAPAT family. (807 aa)
aceBMalate synthase A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the malate synthase family. (533 aa)
metAHomoserine transsuccinylase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. (309 aa)
glmUFused N-acetyl glucosamine-1-phosphate uridyltransferase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. In the C-terminal section; belongs to the transferase hexapeptide repeat family. (456 aa)
CAR20321.1Conserved hypothetical protein, similar to pduL; Involved in 1,2-propanediol (1,2-PD) degradation by catalyzing the conversion of propanoyl-CoA to propanoyl-phosphate. (206 aa)
adhE-3Fragment of fused acetaldehyde-CoA dehydrogenase; Glycine radical enzyme that catalyzes the cleavage of a C-N bond in choline, producing trimethylamine (TMA) and acetaldehyde. Belongs to the glycyl radical enzyme (GRE) family. CutC subfamily. (1140 aa)
cysESerine acetyltransferase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the transferase hexapeptide repeat family. (273 aa)
yiaCPutative acyltransferase with acyl-CoA N-acyltransferase domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (146 aa)
ggtGamma-glutamyltranspeptidase; Function experimentally demonstrated in the studied species; enzyme. (590 aa)
yhbSPutative acyltransferase with acyl-CoA N-acyltransferase domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (167 aa)
tdcEPyruvate formate-lyase 4/2-ketobutyrate formate-lyase; Function experimentally demonstrated in the studied species; enzyme. (764 aa)
gcpO-sialoglycoprotein endopeptidase; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction; Belongs to the KAE1 / TsaD family. (337 aa)
plsC1-acyl-sn-glycerol-3-phosphate acyltransferase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family. (245 aa)
CAR19590.1Putative 8-amino-7-oxononanoate synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (390 aa)
glcBMalate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily. (723 aa)
yqeFAcetyl-CoA acetyltransferase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the thiolase-like superfamily. Thiolase family. (393 aa)
aasFused 2-acylglycerophospho-ethanolamine acyl transferase; 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)
argAFused acetylglutamate kinase homolog (inactive); Function experimentally demonstrated in the studied species; enzyme; Belongs to the acetyltransferase family. ArgA subfamily. (443 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. (387 aa)
rffCTDP-fucosamine acetyltransferase; Catalyzes the acetylation of dTDP-fucosamine (dTDP-4-amino- 4,6-dideoxy-D-galactose) to dTDP-Fuc4NAc, which is utilized in the biosynthesis of the enterobacterial common antigen (ECA). Belongs to the WecD family. (224 aa)
ypfIPutative hydrolase; Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP). (671 aa)
maeBPutative fused malic enzyme oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (759 aa)
eutIPutative phosphotransacetylase subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (338 aa)
ypeAPutative acyltransferase with acyl-CoA N-acyltransferase domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the acetyltransferase family. YpeA subfamily. (141 aa)
ddgPalmitoleoyl-acyl carrier protein (ACP)-dependent acyltransferase; Catalyzes the transfer of palmitoleate from palmitoleoyl-acyl carrier protein (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)- (palmitoleoyl)-lipid IV(A); Belongs to the LpxL/LpxM/LpxP family. LpxP subfamily. (306 aa)
yfcYbeta-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. (436 aa)
fabB3-oxoacyl-[acyl-carrier-protein] synthase I; Function experimentally demonstrated in the studied species; enzyme; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. (406 aa)
ptaPhosphate acetyltransferase; Involved in acetate metabolism. In the N-terminal section; belongs to the CobB/CobQ family. (714 aa)
elaAPutative acyltransferase with acyl-CoA N-acyltransferase domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (155 aa)
atoBacetyl-CoA acetyltransferase; Function experimentally demonstrated in the studied species; carrier; Belongs to the thiolase-like superfamily. Thiolase family. (394 aa)
aatleucyl/phenylalanyl-tRNA-protein transferase; Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl- tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine. (234 aa)
pflBPyruvate formate lyase I; Function experimentally demonstrated in the studied species; enzyme. (760 aa)
mdoCMembrane protein required for modification of periplasmic glucan; Necessary for the succinyl substitution of periplasmic glucans. Could catalyze the transfer of succinyl residues from the cytoplasmic side of the membrane to the nascent glucan backbones on the periplasmic side of the membrane. (385 aa)
lpxLLauryl-acyl carrier protein (ACP)-dependent acyltransferase; Catalyzes the transfer of laurate from lauroyl-acyl carrier protein (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)-(lauroyl)-lipid IV(A). (306 aa)
rimJribosomal-protein-S5-alanine N-acetyltransferase; Function experimentally demonstrated in the studied species; enzyme. (194 aa)
fabH3-oxoacyl-[acyl-carrier-protein] synthase III; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids; Belongs to the thiolase-like superfamily. FabH family. (317 aa)
fabDmalonyl-CoA-[acyl-carrier-protein] transacylase; Function experimentally demonstrated in the studied species; enzyme. (309 aa)
fabF3-oxoacyl-[acyl-carrier-protein] synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. (413 aa)
nhoAN-hydroxyarylamine O-acetyltransferase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the arylamine N-acetyltransferase family. (281 aa)
speGSpermidine N1-acetyltransferase; Function experimentally demonstrated in the studied species; enzyme. (186 aa)
astAArginine succinyltransferase; Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. (344 aa)
lpxMMyristoyl-acyl carrier protein (ACP)-dependent acyltransferase; Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)- lipid A. (323 aa)
yedLPutative acyltransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (159 aa)
wcaBPutative acyl transferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the transferase hexapeptide repeat family. (162 aa)
sucBDihydrolipoyltranssuccinase; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2). (405 aa)
gltACitrate synthase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the citrate synthase family. (427 aa)
lntApolipoprotein N-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation; Belongs to the CN hydrolase family. Apolipoprotein N- acyltransferase subfamily. (512 aa)
lipBLipoyl-protein ligase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. (213 aa)
crcAPalmitoyl transferase for Lipid A; Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors. (186 aa)
yafPPutative acyltransferase with acyl-CoA N-acyltransferase domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (150 aa)
prpC2-methylcitrate synthase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the citrate synthase family. (389 aa)
lacAThiogalactoside acetyltransferase; Function experimentally demonstrated in the studied species; enzyme. (203 aa)
maaMaltose O-acetyltransferase; Function experimentally demonstrated in the studied species; enzyme. (183 aa)
lpxAUDP-N-acetylglucosamine acetyltransferase; Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. (262 aa)
lpxDUDP-3-O-(3-hydroxymyristoyl)-glucosamine N-acyltransferase; Catalyzes the N-acylation of UDP-3-O- (hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell; Belongs to the transferase hexapeptide repeat family. LpxD subfamily. (341 aa)
dapD2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase; Function experimentally demonstrated in the studied species; enzyme. (274 aa)
aceFPyruvate dehydrogenase, dihydrolipoyltransacetylase component E2; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (630 aa)
Your Current Organism:
Escherichia coli IAI39
NCBI taxonomy Id: 585057
Other names: E. coli IAI39
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