node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Hbut_1135 | Hbut_1182 | Hbut_1135 | Hbut_1182 | Site-specific DNA methylase; Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family. | S-adenosylmethionine decarboxylase; Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | 0.900 |
Hbut_1135 | mat | Hbut_1135 | Hbut_0083 | Site-specific DNA methylase; Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family. | S-adenosylmethionine synthetase; Catalyzes the formation of S-adenosylmethionine from methionine and ATP; Belongs to the AdoMet synthase 2 family. | 0.900 |
Hbut_1135 | speH | Hbut_1135 | Hbut_1074 | Site-specific DNA methylase; Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family. | S-adenosylmethionine decarboxylase proenzyme; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | 0.900 |
Hbut_1182 | Hbut_1135 | Hbut_1182 | Hbut_1135 | S-adenosylmethionine decarboxylase; Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | Site-specific DNA methylase; Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family. | 0.900 |
Hbut_1182 | Hbut_1183 | Hbut_1182 | Hbut_1183 | S-adenosylmethionine decarboxylase; Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | Hypothetical protein. | 0.519 |
Hbut_1182 | mat | Hbut_1182 | Hbut_0083 | S-adenosylmethionine decarboxylase; Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | S-adenosylmethionine synthetase; Catalyzes the formation of S-adenosylmethionine from methionine and ATP; Belongs to the AdoMet synthase 2 family. | 0.907 |
Hbut_1182 | speE1 | Hbut_1182 | Hbut_0057 | S-adenosylmethionine decarboxylase; Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | Spermidine synthase, SpeE; Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high- temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to norspermidine, spermidine and norspermine to yield norspermine, thermospermine and caldopentamine, respectively. It can also synthesize sym-norspermidine (bis(3-aminopropyl)amine) f [...] | 0.978 |
Hbut_1182 | speE2 | Hbut_1182 | Hbut_0383 | S-adenosylmethionine decarboxylase; Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | Spermidine synthase; Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high- temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to 1,3-diaminopropane to yield sym-norspermidine (bis(3-aminopropyl)amine). It can also synthesize thermospermine from spermidine with a very low activity. Belongs to the spermidine/spermine [...] | 0.981 |
Hbut_1182 | speH | Hbut_1182 | Hbut_1074 | S-adenosylmethionine decarboxylase; Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | S-adenosylmethionine decarboxylase proenzyme; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | 0.904 |
Hbut_1183 | Hbut_1182 | Hbut_1183 | Hbut_1182 | Hypothetical protein. | S-adenosylmethionine decarboxylase; Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | 0.519 |
mat | Hbut_1135 | Hbut_0083 | Hbut_1135 | S-adenosylmethionine synthetase; Catalyzes the formation of S-adenosylmethionine from methionine and ATP; Belongs to the AdoMet synthase 2 family. | Site-specific DNA methylase; Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family. | 0.900 |
mat | Hbut_1182 | Hbut_0083 | Hbut_1182 | S-adenosylmethionine synthetase; Catalyzes the formation of S-adenosylmethionine from methionine and ATP; Belongs to the AdoMet synthase 2 family. | S-adenosylmethionine decarboxylase; Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | 0.907 |
mat | speH | Hbut_0083 | Hbut_1074 | S-adenosylmethionine synthetase; Catalyzes the formation of S-adenosylmethionine from methionine and ATP; Belongs to the AdoMet synthase 2 family. | S-adenosylmethionine decarboxylase proenzyme; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | 0.907 |
speE1 | Hbut_1182 | Hbut_0057 | Hbut_1182 | Spermidine synthase, SpeE; Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high- temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to norspermidine, spermidine and norspermine to yield norspermine, thermospermine and caldopentamine, respectively. It can also synthesize sym-norspermidine (bis(3-aminopropyl)amine) f [...] | S-adenosylmethionine decarboxylase; Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | 0.978 |
speE1 | speE2 | Hbut_0057 | Hbut_0383 | Spermidine synthase, SpeE; Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high- temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to norspermidine, spermidine and norspermine to yield norspermine, thermospermine and caldopentamine, respectively. It can also synthesize sym-norspermidine (bis(3-aminopropyl)amine) f [...] | Spermidine synthase; Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high- temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to 1,3-diaminopropane to yield sym-norspermidine (bis(3-aminopropyl)amine). It can also synthesize thermospermine from spermidine with a very low activity. Belongs to the spermidine/spermine [...] | 0.907 |
speE1 | speH | Hbut_0057 | Hbut_1074 | Spermidine synthase, SpeE; Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high- temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to norspermidine, spermidine and norspermine to yield norspermine, thermospermine and caldopentamine, respectively. It can also synthesize sym-norspermidine (bis(3-aminopropyl)amine) f [...] | S-adenosylmethionine decarboxylase proenzyme; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | 0.978 |
speE2 | Hbut_1182 | Hbut_0383 | Hbut_1182 | Spermidine synthase; Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high- temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to 1,3-diaminopropane to yield sym-norspermidine (bis(3-aminopropyl)amine). It can also synthesize thermospermine from spermidine with a very low activity. Belongs to the spermidine/spermine [...] | S-adenosylmethionine decarboxylase; Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | 0.981 |
speE2 | speE1 | Hbut_0383 | Hbut_0057 | Spermidine synthase; Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high- temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to 1,3-diaminopropane to yield sym-norspermidine (bis(3-aminopropyl)amine). It can also synthesize thermospermine from spermidine with a very low activity. Belongs to the spermidine/spermine [...] | Spermidine synthase, SpeE; Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high- temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to norspermidine, spermidine and norspermine to yield norspermine, thermospermine and caldopentamine, respectively. It can also synthesize sym-norspermidine (bis(3-aminopropyl)amine) f [...] | 0.907 |
speE2 | speH | Hbut_0383 | Hbut_1074 | Spermidine synthase; Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high- temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to 1,3-diaminopropane to yield sym-norspermidine (bis(3-aminopropyl)amine). It can also synthesize thermospermine from spermidine with a very low activity. Belongs to the spermidine/spermine [...] | S-adenosylmethionine decarboxylase proenzyme; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | 0.981 |
speH | Hbut_1135 | Hbut_1074 | Hbut_1135 | S-adenosylmethionine decarboxylase proenzyme; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. | Site-specific DNA methylase; Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family. | 0.900 |