| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| azo2125 | deaD | azo2125 | azo2122 | Conserved hypothetical protein; TREMBL:Q9HT60:67% identity, 80% similarity to putative hydrolase. Hypothetical protein yqjL. InterPro: Alpha/beta hydrolase fold Pfam: abhydrolase; thioesterase domain uppS: undecaprenyl diphosphate synthase; Specificity unclear. | ATP-dependent RNA helicase; DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation. | 0.466 |
| azo2125 | srkA | azo2125 | azo2124 | Conserved hypothetical protein; TREMBL:Q9HT60:67% identity, 80% similarity to putative hydrolase. Hypothetical protein yqjL. InterPro: Alpha/beta hydrolase fold Pfam: abhydrolase; thioesterase domain uppS: undecaprenyl diphosphate synthase; Specificity unclear. | Conserved hypothetical protein; A protein kinase that phosphorylates Ser and Thr residues. Probably acts to suppress the effects of stress linked to accumulation of reactive oxygen species. Probably involved in the extracytoplasmic stress response. | 0.578 |
| azo2125 | tesA2 | azo2125 | azo2123 | Conserved hypothetical protein; TREMBL:Q9HT60:67% identity, 80% similarity to putative hydrolase. Hypothetical protein yqjL. InterPro: Alpha/beta hydrolase fold Pfam: abhydrolase; thioesterase domain uppS: undecaprenyl diphosphate synthase; Specificity unclear. | Putative acyl-CoA thioesterase. Homology to tesA of E. coli of 32% (sprot|TESA_ECOLI) Hydrolyzes long chain acyl thioesters (c12-c18): 2-lysophosphatidylcholine + h(2)o = glycerophosphocholine + a fatty acid anion. InterPro: GDSL lipolytic enzyme (IPR001087) Pfam: Lipase/Acylhydrolase GDSL-like motif signal peptide no TMH; Family membership. | 0.449 |
| azo3380 | hom | azo3380 | azo2081 | Conserved hypothetical transaminase; Region start changed from 3714581 to 3714479 (102 bases). | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | 0.858 |
| azo3380 | ilvA | azo3380 | azo0500 | Conserved hypothetical transaminase; Region start changed from 3714581 to 3714479 (102 bases). | Probable threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | 0.865 |
| azo3380 | lysC | azo3380 | azo3115 | Conserved hypothetical transaminase; Region start changed from 3714581 to 3714479 (102 bases). | Aspartate kinase (AK) catalyzes the phosphorylation of aspartate. The product of this reaction can then be used in the biosynthesis of lysine or in the pathway leading to homoserine, which participates in the biosynthesis of threonine, isoleucine and methionine. Similar to trembl|Q8RU02 (80%) and to pir|C83531 (74%). Pfam (PF00696): Amino acid kinase family Pfam (PF01842): two ACT domain; High confidence in function and specificity; Belongs to the aspartokinase family. | 0.742 |
| azo3380 | metH | azo3380 | azo3726 | Conserved hypothetical transaminase; Region start changed from 3714581 to 3714479 (102 bases). | Probable methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | 0.929 |
| azo3380 | srkA | azo3380 | azo2124 | Conserved hypothetical transaminase; Region start changed from 3714581 to 3714479 (102 bases). | Conserved hypothetical protein; A protein kinase that phosphorylates Ser and Thr residues. Probably acts to suppress the effects of stress linked to accumulation of reactive oxygen species. Probably involved in the extracytoplasmic stress response. | 0.431 |
| azo3380 | sseA | azo3380 | azo2754 | Conserved hypothetical transaminase; Region start changed from 3714581 to 3714479 (102 bases). | SseA: putative thiosulfate sulfurtransferase (rhodanese-like protein) [EC:2.8.1.1]. This protein 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. Probable 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2) (Rhodanese- like protein) (MST). InterPro: Rhodanese/cdc25 fold; High confidence in function and specificity. | 0.856 |
| deaD | azo2125 | azo2122 | azo2125 | ATP-dependent RNA helicase; DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation. | Conserved hypothetical protein; TREMBL:Q9HT60:67% identity, 80% similarity to putative hydrolase. Hypothetical protein yqjL. InterPro: Alpha/beta hydrolase fold Pfam: abhydrolase; thioesterase domain uppS: undecaprenyl diphosphate synthase; Specificity unclear. | 0.466 |
| deaD | srkA | azo2122 | azo2124 | ATP-dependent RNA helicase; DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation. | Conserved hypothetical protein; A protein kinase that phosphorylates Ser and Thr residues. Probably acts to suppress the effects of stress linked to accumulation of reactive oxygen species. Probably involved in the extracytoplasmic stress response. | 0.587 |
| deaD | tesA2 | azo2122 | azo2123 | ATP-dependent RNA helicase; DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation. | Putative acyl-CoA thioesterase. Homology to tesA of E. coli of 32% (sprot|TESA_ECOLI) Hydrolyzes long chain acyl thioesters (c12-c18): 2-lysophosphatidylcholine + h(2)o = glycerophosphocholine + a fatty acid anion. InterPro: GDSL lipolytic enzyme (IPR001087) Pfam: Lipase/Acylhydrolase GDSL-like motif signal peptide no TMH; Family membership. | 0.775 |
| hom | azo3380 | azo2081 | azo3380 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | Conserved hypothetical transaminase; Region start changed from 3714581 to 3714479 (102 bases). | 0.858 |
| hom | ilvA | azo2081 | azo0500 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | Probable threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | 0.753 |
| hom | lysC | azo2081 | azo3115 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | Aspartate kinase (AK) catalyzes the phosphorylation of aspartate. The product of this reaction can then be used in the biosynthesis of lysine or in the pathway leading to homoserine, which participates in the biosynthesis of threonine, isoleucine and methionine. Similar to trembl|Q8RU02 (80%) and to pir|C83531 (74%). Pfam (PF00696): Amino acid kinase family Pfam (PF01842): two ACT domain; High confidence in function and specificity; Belongs to the aspartokinase family. | 0.984 |
| hom | metH | azo2081 | azo3726 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | Probable methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | 0.971 |
| hom | srkA | azo2081 | azo2124 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | Conserved hypothetical protein; A protein kinase that phosphorylates Ser and Thr residues. Probably acts to suppress the effects of stress linked to accumulation of reactive oxygen species. Probably involved in the extracytoplasmic stress response. | 0.519 |
| hom | sseA | azo2081 | azo2754 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | SseA: putative thiosulfate sulfurtransferase (rhodanese-like protein) [EC:2.8.1.1]. This protein 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. Probable 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2) (Rhodanese- like protein) (MST). InterPro: Rhodanese/cdc25 fold; High confidence in function and specificity. | 0.507 |
| hom | thrC | azo2081 | azo2080 | Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity. | ThrC protein; Threonine synthase is involved in threonine biosynthesis. It catalyses the conversion of O-phospho-L-homoserine and water into L-threonine and orthophosphate,using pyridoxal phosphate as a cofactor. The pyridoxal-phosphate binding site is a Lys (K) residue. The enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. Similar to trembl|Q8XZR7 (68%), to sprot|THRC_METGL (69%) and to sprot|THRC_PSEAE (42%). TIGRFAM: thrC, threonine synthase Pfam (PF00291): Pyridoxal-phosphate dependent enzyme; High confidence in f [...] | 0.988 |
| ilvA | azo3380 | azo0500 | azo3380 | Probable threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | Conserved hypothetical transaminase; Region start changed from 3714581 to 3714479 (102 bases). | 0.865 |