node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ACD16601.1 | ACD17481.1 | Bphyt_2201 | Bphyt_3089 | Hopanoid biosynthesis associated radical SAM protein HpnJ; KEGG: bxe:Bxe_A2062 putative methyltransferase, or Fe-S oxidoreductase; TIGRFAM: hopanoid biosynthesis associated radical SAM protein HpnJ; PFAM: Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB. | Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.480 |
ACD16601.1 | ACD17514.1 | Bphyt_2201 | Bphyt_3122 | Hopanoid biosynthesis associated radical SAM protein HpnJ; KEGG: bxe:Bxe_A2062 putative methyltransferase, or Fe-S oxidoreductase; TIGRFAM: hopanoid biosynthesis associated radical SAM protein HpnJ; PFAM: Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB. | KEGG: bxe:Bxe_A0855 coproporphyrinogen III oxidase; TIGRFAM: oxygen-independent coproporphyrinogen III oxidase; PFAM: Radical SAM domain protein; HemN domain protein; SMART: Elongator protein 3/MiaB/NifB; Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.521 |
ACD17481.1 | ACD16601.1 | Bphyt_3089 | Bphyt_2201 | Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Hopanoid biosynthesis associated radical SAM protein HpnJ; KEGG: bxe:Bxe_A2062 putative methyltransferase, or Fe-S oxidoreductase; TIGRFAM: hopanoid biosynthesis associated radical SAM protein HpnJ; PFAM: Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB. | 0.480 |
ACD17481.1 | miaB | Bphyt_3089 | Bphyt_3329 | Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | tRNA-i(6)A37 thiotransferase enzyme MiaB; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | 0.641 |
ACD17481.1 | rlmN | Bphyt_3089 | Bphyt_2543 | Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Radical SAM enzyme, Cfr family; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. | 0.745 |
ACD17514.1 | ACD16601.1 | Bphyt_3122 | Bphyt_2201 | KEGG: bxe:Bxe_A0855 coproporphyrinogen III oxidase; TIGRFAM: oxygen-independent coproporphyrinogen III oxidase; PFAM: Radical SAM domain protein; HemN domain protein; SMART: Elongator protein 3/MiaB/NifB; Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Hopanoid biosynthesis associated radical SAM protein HpnJ; KEGG: bxe:Bxe_A2062 putative methyltransferase, or Fe-S oxidoreductase; TIGRFAM: hopanoid biosynthesis associated radical SAM protein HpnJ; PFAM: Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB. | 0.521 |
ACD18630.1 | ACD18631.1 | Bphyt_4251 | Bphyt_4252 | PFAM: Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB; KEGG: cps:CPS_4049 FO synthase subunit 1. | PFAM: Radical SAM domain protein; KEGG: pde:Pden_1115 radical SAM domain protein. | 0.998 |
ACD18631.1 | ACD18630.1 | Bphyt_4252 | Bphyt_4251 | PFAM: Radical SAM domain protein; KEGG: pde:Pden_1115 radical SAM domain protein. | PFAM: Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB; KEGG: cps:CPS_4049 FO synthase subunit 1. | 0.998 |
lipA | lipA-2 | Bphyt_0504 | Bphyt_5917 | Lipoic acid synthetase; 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. | Lipoic acid synthetase; 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. | 0.903 |
lipA-2 | lipA | Bphyt_5917 | Bphyt_0504 | Lipoic acid synthetase; 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. | Lipoic acid synthetase; 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. | 0.903 |
miaB | ACD17481.1 | Bphyt_3329 | Bphyt_3089 | tRNA-i(6)A37 thiotransferase enzyme MiaB; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.641 |
miaB | rlmN | Bphyt_3329 | Bphyt_2543 | tRNA-i(6)A37 thiotransferase enzyme MiaB; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | Radical SAM enzyme, Cfr family; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. | 0.792 |
rimO | rlmN | Bphyt_1848 | Bphyt_2543 | MiaB-like tRNA modifying enzyme YliG; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. | Radical SAM enzyme, Cfr family; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. | 0.569 |
rlmN | ACD17481.1 | Bphyt_2543 | Bphyt_3089 | Radical SAM enzyme, Cfr family; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. | Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.745 |
rlmN | miaB | Bphyt_2543 | Bphyt_3329 | Radical SAM enzyme, Cfr family; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. | tRNA-i(6)A37 thiotransferase enzyme MiaB; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | 0.792 |
rlmN | rimO | Bphyt_2543 | Bphyt_1848 | Radical SAM enzyme, Cfr family; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. | MiaB-like tRNA modifying enzyme YliG; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. | 0.569 |