| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ACN13132.1 | hemN2 | HRM2_00090 | HRM2_32990 | Conserved hypothetical protein; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. | HemN2; 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. | 0.679 |
| ACN13132.1 | miaB | HRM2_00090 | HRM2_21710 | Conserved hypothetical protein; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. | 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. | 0.746 |
| ACN16375.1 | hemN2 | HRM2_33000 | HRM2_32990 | Putative oxygen-independent coproporphyrinogen III oxidase. | HemN2; 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. | 0.847 |
| ACN16375.1 | mltG | HRM2_33000 | HRM2_33010 | Putative oxygen-independent coproporphyrinogen III oxidase. | Putative aminodeoxychorismate lyase; Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. Belongs to the transglycosylase MltG family. | 0.564 |
| fixN | fixO | HRM2_15110 | HRM2_15100 | FixN; Cytochrome C oxidase, polypeptide subunit FixN (cytochrome cbb3, subunit 1). | FixO; Cytochrome C oxidase, mono-heme subunit FixO. | 0.999 |
| fixN | hemN2 | HRM2_15110 | HRM2_32990 | FixN; Cytochrome C oxidase, polypeptide subunit FixN (cytochrome cbb3, subunit 1). | HemN2; 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. | 0.649 |
| fixO | fixN | HRM2_15100 | HRM2_15110 | FixO; Cytochrome C oxidase, mono-heme subunit FixO. | FixN; Cytochrome C oxidase, polypeptide subunit FixN (cytochrome cbb3, subunit 1). | 0.999 |
| fixO | hemN2 | HRM2_15100 | HRM2_32990 | FixO; Cytochrome C oxidase, mono-heme subunit FixO. | HemN2; 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. | 0.766 |
| flgF | hemN2 | HRM2_37030 | HRM2_32990 | FlgF; Flagellar basal-body rod protein FlgF. | HemN2; 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. | 0.592 |
| flgF | mltG | HRM2_37030 | HRM2_33010 | FlgF; Flagellar basal-body rod protein FlgF. | Putative aminodeoxychorismate lyase; Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. Belongs to the transglycosylase MltG family. | 0.592 |
| hemD | hemN2 | HRM2_35960 | HRM2_32990 | HemD; Porphyrin biosynthesis protein HemD [includes: uroporphyrin-III C-methyltransferase; uroporphyrinogen-III synthase]. | HemN2; 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. | 0.630 |
| hemD | miaB | HRM2_35960 | HRM2_21710 | HemD; Porphyrin biosynthesis protein HemD [includes: uroporphyrin-III C-methyltransferase; uroporphyrinogen-III 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. | 0.431 |
| hemN2 | ACN13132.1 | HRM2_32990 | HRM2_00090 | HemN2; 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. | Conserved hypothetical protein; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. | 0.679 |
| hemN2 | ACN16375.1 | HRM2_32990 | HRM2_33000 | HemN2; 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. | Putative oxygen-independent coproporphyrinogen III oxidase. | 0.847 |
| hemN2 | fixN | HRM2_32990 | HRM2_15110 | HemN2; 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. | FixN; Cytochrome C oxidase, polypeptide subunit FixN (cytochrome cbb3, subunit 1). | 0.649 |
| hemN2 | fixO | HRM2_32990 | HRM2_15100 | HemN2; 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. | FixO; Cytochrome C oxidase, mono-heme subunit FixO. | 0.766 |
| hemN2 | flgF | HRM2_32990 | HRM2_37030 | HemN2; 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. | FlgF; Flagellar basal-body rod protein FlgF. | 0.592 |
| hemN2 | hemD | HRM2_32990 | HRM2_35960 | HemN2; 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. | HemD; Porphyrin biosynthesis protein HemD [includes: uroporphyrin-III C-methyltransferase; uroporphyrinogen-III synthase]. | 0.630 |
| hemN2 | lepA | HRM2_32990 | HRM2_20920 | HemN2; 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. | LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | 0.795 |
| hemN2 | miaB | HRM2_32990 | HRM2_21710 | HemN2; 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. | 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 |