| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ALO48339.1 | ALO48406.1 | AS203_03950 | AS203_04345 | tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))- methylthiotransferase MtaB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.464 |
| ALO48339.1 | rlmN | AS203_03950 | AS203_07705 | tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))- methylthiotransferase MtaB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 23S rRNA (adenine(2503)-C2)-methyltransferase; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs; Belongs to the radical SAM superfamily. RlmN family. | 0.517 |
| ALO48393.1 | ALO48406.1 | AS203_04280 | AS203_04345 | Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.615 |
| ALO48393.1 | secF | AS203_04280 | AS203_00225 | Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Preprotein translocase subunit SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA; Belongs to the SecD/SecF family. SecD subfamily. | 0.422 |
| ALO48405.1 | ALO48406.1 | AS203_04340 | AS203_04345 | Elongation factor G; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.660 |
| ALO48405.1 | secF | AS203_04340 | AS203_00225 | Elongation factor G; Derived by automated computational analysis using gene prediction method: Protein Homology. | Preprotein translocase subunit SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA; Belongs to the SecD/SecF family. SecD subfamily. | 0.424 |
| ALO48406.1 | ALO48339.1 | AS203_04345 | AS203_03950 | 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 (N(6)-L-threonylcarbamoyladenosine(37)-C(2))- methylthiotransferase MtaB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.464 |
| ALO48406.1 | ALO48393.1 | AS203_04345 | AS203_04280 | 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. | Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.615 |
| ALO48406.1 | ALO48405.1 | AS203_04345 | AS203_04340 | 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. | Elongation factor G; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.660 |
| ALO48406.1 | ALO48666.1 | AS203_04345 | AS203_05890 | 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. | YgiQ family radical SAM protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.450 |
| ALO48406.1 | ALO49395.1 | AS203_04345 | AS203_10070 | 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. | Protoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. | 0.441 |
| ALO48406.1 | ALO49873.1 | AS203_04345 | AS203_05425 | 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.429 |
| ALO48406.1 | miaB | AS203_04345 | AS203_11740 | 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-2-methylthio-N(6)-dimethylallyladenosine synthase 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. | 0.464 |
| ALO48406.1 | rimO | AS203_04345 | AS203_05995 | 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. | Ribosomal protein S12 methylthiotransferase RimO; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. | 0.436 |
| ALO48406.1 | rlmN | AS203_04345 | AS203_07705 | 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. | 23S rRNA (adenine(2503)-C2)-methyltransferase; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs; Belongs to the radical SAM superfamily. RlmN family. | 0.608 |
| ALO48406.1 | secF | AS203_04345 | AS203_00225 | 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. | Preprotein translocase subunit SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA; Belongs to the SecD/SecF family. SecD subfamily. | 0.435 |
| ALO48666.1 | ALO48406.1 | AS203_05890 | AS203_04345 | YgiQ family radical SAM protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.450 |
| ALO49395.1 | ALO48406.1 | AS203_10070 | AS203_04345 | Protoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. | 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. | 0.441 |
| ALO49873.1 | ALO48406.1 | AS203_05425 | AS203_04345 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.429 |
| miaB | ALO48406.1 | AS203_11740 | AS203_04345 | tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase 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. | 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. | 0.464 |