node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
dcyD | fliY | b1919 | b1920 | D-cysteine desulfhydrase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D- alanine. | Cystine transporter subunit; Part of the ABC transporter complex FliY-YecC-YecS involved in L-cystine transport. The system can probably also transport L- cysteine, and it mediates accumulation of the toxic compounds L- selenaproline (SCA) and L-selenocystine (SeCys). Binds cystine ; Belongs to the bacterial solute-binding protein 3 family. | 0.925 |
dcyD | fliZ | b1919 | b1921 | D-cysteine desulfhydrase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D- alanine. | RpoS antagonist; During the post-exponential growth phase transiently interferes with RpoS (sigma S) activity without affecting expression of RpoS itself. It is probably not an anti-sigma factor as its overexpression is detrimental in rapidly growing cells where there is almost no sigma S factor. There is a strong overlap between Crl- activated genes and FliZ-down-regulated genes. FliZ acts as a timing device for expression of the genes for the adhesive curli fimbriae by indirectly decreasing expression of the curli regulator CsgD. | 0.504 |
dcyD | malY | b1919 | b1622 | D-cysteine desulfhydrase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D- alanine. | PLP-dependent beta-cystathionase and maltose regulon regulator; Acts as a beta-cystathionase and as a repressor of the maltose regulon. | 0.905 |
dcyD | metC | b1919 | b3008 | D-cysteine desulfhydrase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D- alanine. | Cystathionine beta-lyase, PLP-dependent; Primarily catalyzes the cleavage of cystathionine to homocysteine, pyruvate and ammonia during methionine biosynthesis. Also exhibits cysteine desulfhydrase activity, producing sulfide from cysteine. In addition, under certain growth conditions, exhibits significant alanine racemase coactivity. | 0.905 |
dcyD | solA | b1919 | b1059 | D-cysteine desulfhydrase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D- alanine. | N-methyltryptophan oxidase, FAD-binding; Catalyzes the oxidative demethylation of N-methyl-L- tryptophan. Can also use other N-methyl amino acids, including sarcosine, which, however, is a poor substrate. | 0.534 |
dcyD | sseA | b1919 | b2521 | D-cysteine desulfhydrase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D- alanine. | 3-mercaptopyruvate sulfurtransferase; Transfers a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity (130-fold lower). Its participation in detoxification of cyanide may be small. May be involved in the enhancement of serine sensitivity. | 0.900 |
dcyD | ydjN | b1919 | b1729 | D-cysteine desulfhydrase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D- alanine. | Putative transporter; Involved in L-cystine transport. Can probably also transport L-cysteine. Mediates accumulation of the toxic compounds L- selenaproline (SCA) and L-selenocystine (SeCys). Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family. | 0.575 |
dcyD | yecC | b1919 | b1917 | D-cysteine desulfhydrase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D- alanine. | Putative ABC transporter ATPase; Part of the ABC transporter complex FliY-YecC-YecS involved in L-cystine transport. The system can probably also transport L- cysteine, and it mediates accumulation of the toxic compounds L- selenaproline (SCA) and L-selenocystine (SeCys). Probably responsible for energy coupling to the transport system (Probable). | 0.920 |
dcyD | yecS | b1919 | b1918 | D-cysteine desulfhydrase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D- alanine. | ABC family putative inner membrane permease; Part of the ABC transporter complex FliY-YecC-YecS involved in L-cystine transport. The system can probably also transport L- cysteine, and it mediates accumulation of the toxic compounds L- selenaproline (SCA) and L-selenocystine (SeCys). Probably responsible for the translocation of the substrate across the membrane (Probable). | 0.960 |
dcyD | ygeX | b1919 | b2871 | D-cysteine desulfhydrase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D- alanine. | 2,3-diaminopropionate ammonia lyase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro the D-isomer of serine is degraded to pyruvate, though very poorly; other amino acids (L-serine, D- and L-threonine, D- and L-beta- Cl-alanine) are not substrates. In vivo allows poor growth on L-DAP or a DL-DAP mixture but not on D-DAP alone, this may be due to a poor promoter. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, [...] | 0.446 |
fliY | dcyD | b1920 | b1919 | Cystine transporter subunit; Part of the ABC transporter complex FliY-YecC-YecS involved in L-cystine transport. The system can probably also transport L- cysteine, and it mediates accumulation of the toxic compounds L- selenaproline (SCA) and L-selenocystine (SeCys). Binds cystine ; Belongs to the bacterial solute-binding protein 3 family. | D-cysteine desulfhydrase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D- alanine. | 0.925 |
fliY | fliZ | b1920 | b1921 | Cystine transporter subunit; Part of the ABC transporter complex FliY-YecC-YecS involved in L-cystine transport. The system can probably also transport L- cysteine, and it mediates accumulation of the toxic compounds L- selenaproline (SCA) and L-selenocystine (SeCys). Binds cystine ; Belongs to the bacterial solute-binding protein 3 family. | RpoS antagonist; During the post-exponential growth phase transiently interferes with RpoS (sigma S) activity without affecting expression of RpoS itself. It is probably not an anti-sigma factor as its overexpression is detrimental in rapidly growing cells where there is almost no sigma S factor. There is a strong overlap between Crl- activated genes and FliZ-down-regulated genes. FliZ acts as a timing device for expression of the genes for the adhesive curli fimbriae by indirectly decreasing expression of the curli regulator CsgD. | 0.827 |
fliY | ydjN | b1920 | b1729 | Cystine transporter subunit; Part of the ABC transporter complex FliY-YecC-YecS involved in L-cystine transport. The system can probably also transport L- cysteine, and it mediates accumulation of the toxic compounds L- selenaproline (SCA) and L-selenocystine (SeCys). Binds cystine ; Belongs to the bacterial solute-binding protein 3 family. | Putative transporter; Involved in L-cystine transport. Can probably also transport L-cysteine. Mediates accumulation of the toxic compounds L- selenaproline (SCA) and L-selenocystine (SeCys). Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family. | 0.782 |
fliY | yecC | b1920 | b1917 | Cystine transporter subunit; Part of the ABC transporter complex FliY-YecC-YecS involved in L-cystine transport. The system can probably also transport L- cysteine, and it mediates accumulation of the toxic compounds L- selenaproline (SCA) and L-selenocystine (SeCys). Binds cystine ; Belongs to the bacterial solute-binding protein 3 family. | Putative ABC transporter ATPase; Part of the ABC transporter complex FliY-YecC-YecS involved in L-cystine transport. The system can probably also transport L- cysteine, and it mediates accumulation of the toxic compounds L- selenaproline (SCA) and L-selenocystine (SeCys). Probably responsible for energy coupling to the transport system (Probable). | 0.999 |
fliY | yecS | b1920 | b1918 | Cystine transporter subunit; Part of the ABC transporter complex FliY-YecC-YecS involved in L-cystine transport. The system can probably also transport L- cysteine, and it mediates accumulation of the toxic compounds L- selenaproline (SCA) and L-selenocystine (SeCys). Binds cystine ; Belongs to the bacterial solute-binding protein 3 family. | ABC family putative inner membrane permease; Part of the ABC transporter complex FliY-YecC-YecS involved in L-cystine transport. The system can probably also transport L- cysteine, and it mediates accumulation of the toxic compounds L- selenaproline (SCA) and L-selenocystine (SeCys). Probably responsible for the translocation of the substrate across the membrane (Probable). | 0.999 |
fliZ | dcyD | b1921 | b1919 | RpoS antagonist; During the post-exponential growth phase transiently interferes with RpoS (sigma S) activity without affecting expression of RpoS itself. It is probably not an anti-sigma factor as its overexpression is detrimental in rapidly growing cells where there is almost no sigma S factor. There is a strong overlap between Crl- activated genes and FliZ-down-regulated genes. FliZ acts as a timing device for expression of the genes for the adhesive curli fimbriae by indirectly decreasing expression of the curli regulator CsgD. | D-cysteine desulfhydrase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D- alanine. | 0.504 |
fliZ | fliY | b1921 | b1920 | RpoS antagonist; During the post-exponential growth phase transiently interferes with RpoS (sigma S) activity without affecting expression of RpoS itself. It is probably not an anti-sigma factor as its overexpression is detrimental in rapidly growing cells where there is almost no sigma S factor. There is a strong overlap between Crl- activated genes and FliZ-down-regulated genes. FliZ acts as a timing device for expression of the genes for the adhesive curli fimbriae by indirectly decreasing expression of the curli regulator CsgD. | Cystine transporter subunit; Part of the ABC transporter complex FliY-YecC-YecS involved in L-cystine transport. The system can probably also transport L- cysteine, and it mediates accumulation of the toxic compounds L- selenaproline (SCA) and L-selenocystine (SeCys). Binds cystine ; Belongs to the bacterial solute-binding protein 3 family. | 0.827 |
malY | dcyD | b1622 | b1919 | PLP-dependent beta-cystathionase and maltose regulon regulator; Acts as a beta-cystathionase and as a repressor of the maltose regulon. | D-cysteine desulfhydrase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D- alanine. | 0.905 |
malY | metC | b1622 | b3008 | PLP-dependent beta-cystathionase and maltose regulon regulator; Acts as a beta-cystathionase and as a repressor of the maltose regulon. | Cystathionine beta-lyase, PLP-dependent; Primarily catalyzes the cleavage of cystathionine to homocysteine, pyruvate and ammonia during methionine biosynthesis. Also exhibits cysteine desulfhydrase activity, producing sulfide from cysteine. In addition, under certain growth conditions, exhibits significant alanine racemase coactivity. | 0.985 |
malY | sseA | b1622 | b2521 | PLP-dependent beta-cystathionase and maltose regulon regulator; Acts as a beta-cystathionase and as a repressor of the maltose regulon. | 3-mercaptopyruvate sulfurtransferase; Transfers a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity (130-fold lower). Its participation in detoxification of cyanide may be small. May be involved in the enhancement of serine sensitivity. | 0.923 |