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fadH fadH accB accB bioH bioH acpT acpT fadA fadA entD entD lipA lipA lipB lipB sucC sucC bioC bioC smtA smtA fabA fabA plsX plsX fabF fabF fadR fadR fadD fadD fabB fabB fadB fadB fabH fabH tpiA tpiA yijC yijC plsB plsB tesA tesA tesB tesB yafH yafH yajB yajB fabZ fabZ fadL fadL aas aas ygiH ygiH
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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
filled nodes:
a 3D structure is known or predicted
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experimentally determined
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fadH2,4-dieonyl-coa reductase; Similar to E. coli putative NADPH dehydrogenase (AAC76116.1); Blastp hit to AAC76116.1 (672 aa), 85% identity in aa 1 - 672. (672 aa)
accBacetylCoA carboxylase, BCCP subunit; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. (156 aa)
bioHPutative hydrolase; The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. (256 aa)
acpTPutative phosphopantetheinyl transferase; May be involved in an alternative pathway for phosphopantetheinyl transfer and holo-ACP synthesis. The native apo- protein substrate is unknown; Belongs to the P-Pant transferase superfamily. Gsp/Sfp/HetI/AcpT family. (192 aa)
fadA3-ketoacyl-CoA thiolase; 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 (By similarity). (387 aa)
entDEnterochelin synthetase, component D (phoshpantetheinyltransferase); Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3- dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo- domains of both EntB (ArCP domain) and EntF (PC [...] (234 aa)
lipALipoate synthase, an iron-sulfur enzyme; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. (321 aa)
lipBPutative ligase in lipoate biosynthesis; 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. (191 aa)
sucCsuccinyl-CoA synthetase, beta subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. (388 aa)
bioCBiotin biosynthesis; Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L- methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway. (251 aa)
smtAS-adenosylmethionine-dependent methyltransferase; Catalyzes the methylation of 5-carboxymethoxyuridine (cmo5U) to form 5-methoxycarbonylmethoxyuridine (mcmo5U) at position 34 in tRNAs; Belongs to the class I-like SAM-binding methyltransferase superfamily. CmoM family. (267 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. (172 aa)
plsXPutative fatty acid/phospholipid synthesis protein; Catalyzes the reversible formation of acyl-phosphate (acyl- PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. (359 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)
fadRNegative regulator of fad regulon; 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. Binding of FadR is specifically inhibited by long chain fatty acyl-CoA compounds (By similarity). (239 aa)
fadDacyl-CoA synthetase; Catalyzes the esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids; Belongs to the ATP-dependent AMP-binding enzyme family. (561 aa)
fabBSimilar to E. coli 3-oxoacyl-[acyl-carrier-protein] synthase I (AAC75383.1); Blastp hit to AAC75383.1 (406 aa), 96% identity in aa 1 - 404; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. (404 aa)
fadB3-hydroxyacyl-coA dehydrogenase of 4-enzyme FadB protein; 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)
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)
tpiATriosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family. (255 aa)
yijCPutative TetR/AcrR family transcriptional repressor; Represses the transcription of fabB, involved in unsaturated fatty acid (UFA) biosynthesis. By controlling UFA production, FabR directly influences the physical properties of the membrane bilayer. (211 aa)
plsBGlycerolphosphate acyltransferase activity; Similar to E. coli glycerol-3-phosphate acyltransferase (AAC77011.1); Blastp hit to AAC77011.1 (827 aa), 94% identity in aa 21 - 826; Belongs to the GPAT/DAPAT family. (806 aa)
tesASimilar to E. coli acyl-CoA thioesterase I; also functions as protease I (AAC73596.1); Blastp hit to AAC73596.1 (208 aa), 89% identity in aa 2 - 205. (204 aa)
tesBSimilar to E. coli acyl-CoA thioesterase II (AAC73555.1); Blastp hit to AAC73555.1 (286 aa), 91% identity in aa 1 - 286. (286 aa)
yafHPutative acyl-CoA 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 S.typhimurium to utilize medium- and long-chain fatty acids as sole carbon sources for growth. Is needed for bacterial survival during carbone-source starvation. (814 aa)
yajBPutative cytoplasmic protein; Converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine prosthetic group from ACP; Belongs to the AcpH family. (193 aa)
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 (By similarity). (151 aa)
fadLTransport of long-chain fatty acids; Involved in translocation of long-chain fatty acids across the outer membrane. FadL may form a specific channel (By similarity). Belongs to the OmpP1/FadL family. (437 aa)
aas2-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)
ygiHPutative inner membrane protein; Catalyzes the transfer of an acyl group from acyl-ACP to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme can also utilize acyl-CoA as fatty acyl donor, but not acyl- PO(4); Belongs to the PlsY family. (203 aa)
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
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