| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KXB77487.1 | KXB79590.1 | HMPREF1860_01384 | HMPREF1860_00587 | Protoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. | KEGG: pmz:HMPREF0659_A5198 6.5e-141 hemN; coproporphyrinogen dehydrogenase K02495; Psort location: Cytoplasmic, score: 9.97. | 0.835 |
| KXB77487.1 | KXB81932.1 | HMPREF1860_01384 | HMPREF1860_00026 | Protoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. | Putative 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. | 0.607 |
| KXB78030.1 | KXB79590.1 | HMPREF1860_01072 | HMPREF1860_00587 | Pyruvate synthase; KEGG: pdn:HMPREF9137_1524 0. nifJ; pyruvate synthase K03737; Psort location: Cytoplasmic, score: 8.96. | KEGG: pmz:HMPREF0659_A5198 6.5e-141 hemN; coproporphyrinogen dehydrogenase K02495; Psort location: Cytoplasmic, score: 9.97. | 0.562 |
| KXB78030.1 | KXB81932.1 | HMPREF1860_01072 | HMPREF1860_00026 | Pyruvate synthase; KEGG: pdn:HMPREF9137_1524 0. nifJ; pyruvate synthase K03737; Psort location: Cytoplasmic, score: 8.96. | Putative 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. | 0.502 |
| KXB79590.1 | KXB77487.1 | HMPREF1860_00587 | HMPREF1860_01384 | KEGG: pmz:HMPREF0659_A5198 6.5e-141 hemN; coproporphyrinogen dehydrogenase K02495; Psort location: Cytoplasmic, score: 9.97. | Protoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. | 0.835 |
| KXB79590.1 | KXB78030.1 | HMPREF1860_00587 | HMPREF1860_01072 | KEGG: pmz:HMPREF0659_A5198 6.5e-141 hemN; coproporphyrinogen dehydrogenase K02495; Psort location: Cytoplasmic, score: 9.97. | Pyruvate synthase; KEGG: pdn:HMPREF9137_1524 0. nifJ; pyruvate synthase K03737; Psort location: Cytoplasmic, score: 8.96. | 0.562 |
| KXB79590.1 | KXB81932.1 | HMPREF1860_00587 | HMPREF1860_00026 | KEGG: pmz:HMPREF0659_A5198 6.5e-141 hemN; coproporphyrinogen dehydrogenase K02495; Psort location: Cytoplasmic, score: 9.97. | Putative 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. | 0.524 |
| KXB81931.1 | KXB81932.1 | HMPREF1860_00025 | HMPREF1860_00026 | Hypothetical protein; KEGG: scc:Spico_0970 0.0052 membrane protease FtsH catalytic subunit; K03798 cell division protease FtsH; Psort location: CytoplasmicMembrane, score: 9.82. | Putative 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. | 0.783 |
| KXB81931.1 | KXB81933.1 | HMPREF1860_00025 | HMPREF1860_00027 | Hypothetical protein; KEGG: scc:Spico_0970 0.0052 membrane protease FtsH catalytic subunit; K03798 cell division protease FtsH; Psort location: CytoplasmicMembrane, score: 9.82. | KEGG: ddf:DEFDS_1775 1.3e-110 translation elongation factor G K02355; Psort location: Cytoplasmic, score: 9.97. | 0.617 |
| KXB81932.1 | KXB77487.1 | HMPREF1860_00026 | HMPREF1860_01384 | Putative 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. | Protoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. | 0.607 |
| KXB81932.1 | KXB78030.1 | HMPREF1860_00026 | HMPREF1860_01072 | Putative 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. | Pyruvate synthase; KEGG: pdn:HMPREF9137_1524 0. nifJ; pyruvate synthase K03737; Psort location: Cytoplasmic, score: 8.96. | 0.502 |
| KXB81932.1 | KXB79590.1 | HMPREF1860_00026 | HMPREF1860_00587 | Putative 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. | KEGG: pmz:HMPREF0659_A5198 6.5e-141 hemN; coproporphyrinogen dehydrogenase K02495; Psort location: Cytoplasmic, score: 9.97. | 0.524 |
| KXB81932.1 | KXB81931.1 | HMPREF1860_00026 | HMPREF1860_00025 | Putative 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. | Hypothetical protein; KEGG: scc:Spico_0970 0.0052 membrane protease FtsH catalytic subunit; K03798 cell division protease FtsH; Psort location: CytoplasmicMembrane, score: 9.82. | 0.783 |
| KXB81932.1 | KXB81933.1 | HMPREF1860_00026 | HMPREF1860_00027 | Putative 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. | KEGG: ddf:DEFDS_1775 1.3e-110 translation elongation factor G K02355; Psort location: Cytoplasmic, score: 9.97. | 0.672 |
| KXB81932.1 | miaB | HMPREF1860_00026 | HMPREF1860_00341 | Putative 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. | 0.447 |
| KXB81932.1 | pnp | HMPREF1860_00026 | HMPREF1860_00323 | Putative 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. | Polyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction. | 0.400 |
| KXB81932.1 | rlmN | HMPREF1860_00026 | HMPREF1860_00774 | Putative 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. | 23S rRNA 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. | 0.566 |
| KXB81933.1 | KXB81931.1 | HMPREF1860_00027 | HMPREF1860_00025 | KEGG: ddf:DEFDS_1775 1.3e-110 translation elongation factor G K02355; Psort location: Cytoplasmic, score: 9.97. | Hypothetical protein; KEGG: scc:Spico_0970 0.0052 membrane protease FtsH catalytic subunit; K03798 cell division protease FtsH; Psort location: CytoplasmicMembrane, score: 9.82. | 0.617 |
| KXB81933.1 | KXB81932.1 | HMPREF1860_00027 | HMPREF1860_00026 | KEGG: ddf:DEFDS_1775 1.3e-110 translation elongation factor G K02355; Psort location: Cytoplasmic, score: 9.97. | Putative 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. | 0.672 |
| KXB81933.1 | pnp | HMPREF1860_00027 | HMPREF1860_00323 | KEGG: ddf:DEFDS_1775 1.3e-110 translation elongation factor G K02355; Psort location: Cytoplasmic, score: 9.97. | Polyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction. | 0.636 |