| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SO_4399 | SO_4400 | SO_4399 | SO_4400 | Protein of unknown function. | Prolyl aminopeptidase S33 family; Belongs to the peptidase S33 family. | 0.773 |
| SO_4399 | dtd | SO_4399 | SO_4398 | Protein of unknown function. | D-tyrosyl-tRNA(Tyr) deacylase Dtd; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | 0.756 |
| SO_4399 | yiiD | SO_4399 | SO_4397 | Protein of unknown function. | Thioesterase domain protein YiiD. | 0.678 |
| SO_4400 | SO_4399 | SO_4400 | SO_4399 | Prolyl aminopeptidase S33 family; Belongs to the peptidase S33 family. | Protein of unknown function. | 0.773 |
| SO_4400 | dtd | SO_4400 | SO_4398 | Prolyl aminopeptidase S33 family; Belongs to the peptidase S33 family. | D-tyrosyl-tRNA(Tyr) deacylase Dtd; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | 0.817 |
| SO_4400 | yiiD | SO_4400 | SO_4397 | Prolyl aminopeptidase S33 family; Belongs to the peptidase S33 family. | Thioesterase domain protein YiiD. | 0.674 |
| acpS | fabH | SO_1352 | SO_2778 | Holo-(acyl-carrier protein) synthase AcpS; Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein; Belongs to the P-Pant transferase superfamily. AcpS family. | 3-oxoacyl-(acyl-carrier-protein) synthase III FabH; 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. | 0.624 |
| acpS | yiiD | SO_1352 | SO_4397 | Holo-(acyl-carrier protein) synthase AcpS; Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein; Belongs to the P-Pant transferase superfamily. AcpS family. | Thioesterase domain protein YiiD. | 0.809 |
| dtd | SO_4399 | SO_4398 | SO_4399 | D-tyrosyl-tRNA(Tyr) deacylase Dtd; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | Protein of unknown function. | 0.756 |
| dtd | SO_4400 | SO_4398 | SO_4400 | D-tyrosyl-tRNA(Tyr) deacylase Dtd; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | Prolyl aminopeptidase S33 family; Belongs to the peptidase S33 family. | 0.817 |
| dtd | yiiD | SO_4398 | SO_4397 | D-tyrosyl-tRNA(Tyr) deacylase Dtd; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | Thioesterase domain protein YiiD. | 0.948 |
| fabH | acpS | SO_2778 | SO_1352 | 3-oxoacyl-(acyl-carrier-protein) synthase III FabH; 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. | Holo-(acyl-carrier protein) synthase AcpS; Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein; Belongs to the P-Pant transferase superfamily. AcpS family. | 0.624 |
| fabH | glmU | SO_2778 | SO_4745 | 3-oxoacyl-(acyl-carrier-protein) synthase III FabH; 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. | Glucosamine-1-phosphate N-acetyltransferase; 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. | 0.406 |
| fabH | yiiD | SO_2778 | SO_4397 | 3-oxoacyl-(acyl-carrier-protein) synthase III FabH; 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. | Thioesterase domain protein YiiD. | 0.577 |
| glmU | fabH | SO_4745 | SO_2778 | Glucosamine-1-phosphate N-acetyltransferase; 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. | 3-oxoacyl-(acyl-carrier-protein) synthase III FabH; 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. | 0.406 |
| glmU | yiiD | SO_4745 | SO_4397 | Glucosamine-1-phosphate N-acetyltransferase; 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. | Thioesterase domain protein YiiD. | 0.803 |
| metJ | syd | SO_4057 | SO_1609 | Transcriptional repressor of methionine metabolism MetJ; This regulatory protein, when combined with SAM (S- adenosylmethionine) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis; Belongs to the MetJ family. | SecY binding protein Syd; Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. Belongs to the Syd family. | 0.716 |
| metJ | yiiD | SO_4057 | SO_4397 | Transcriptional repressor of methionine metabolism MetJ; This regulatory protein, when combined with SAM (S- adenosylmethionine) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis; Belongs to the MetJ family. | Thioesterase domain protein YiiD. | 0.560 |
| syd | metJ | SO_1609 | SO_4057 | SecY binding protein Syd; Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. Belongs to the Syd family. | Transcriptional repressor of methionine metabolism MetJ; This regulatory protein, when combined with SAM (S- adenosylmethionine) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis; Belongs to the MetJ family. | 0.716 |
| syd | yiiD | SO_1609 | SO_4397 | SecY binding protein Syd; Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. Belongs to the Syd family. | Thioesterase domain protein YiiD. | 0.550 |