node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Clim_1937 | Clim_2042 | Clim_1937 | Clim_2042 | PFAM: glutamine amidotransferase class-II; glutamate synthase alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase; KEGG: cph:Cpha266_0628 glutamate synthase (NADH) large subunit. | KEGG: cph:Cpha266_2083 citrate synthase; TIGRFAM: citrate synthase I; PFAM: Citrate synthase; Belongs to the citrate synthase family. | 0.902 |
Clim_1937 | gatA | Clim_1937 | Clim_0332 | PFAM: glutamine amidotransferase class-II; glutamate synthase alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase; KEGG: cph:Cpha266_0628 glutamate synthase (NADH) large subunit. | glutamyl-tRNA(Gln) amidotransferase, A subunit; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). | 0.718 |
Clim_1937 | gatB | Clim_1937 | Clim_2287 | PFAM: glutamine amidotransferase class-II; glutamate synthase alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase; KEGG: cph:Cpha266_0628 glutamate synthase (NADH) large subunit. | glutamyl-tRNA(Gln) amidotransferase, B subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.673 |
Clim_1937 | gatC | Clim_1937 | Clim_2041 | PFAM: glutamine amidotransferase class-II; glutamate synthase alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase; KEGG: cph:Cpha266_0628 glutamate synthase (NADH) large subunit. | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.687 |
Clim_2040 | Clim_2042 | Clim_2040 | Clim_2042 | PFAM: protein of unknown function DUF167; KEGG: cph:Cpha266_2081 protein of unknown function DUF167; Belongs to the UPF0235 family. | KEGG: cph:Cpha266_2083 citrate synthase; TIGRFAM: citrate synthase I; PFAM: Citrate synthase; Belongs to the citrate synthase family. | 0.682 |
Clim_2040 | dtd | Clim_2040 | Clim_2039 | PFAM: protein of unknown function DUF167; KEGG: cph:Cpha266_2081 protein of unknown function DUF167; Belongs to the UPF0235 family. | D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | 0.777 |
Clim_2040 | gatC | Clim_2040 | Clim_2041 | PFAM: protein of unknown function DUF167; KEGG: cph:Cpha266_2081 protein of unknown function DUF167; Belongs to the UPF0235 family. | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.763 |
Clim_2040 | kdsB | Clim_2040 | Clim_2038 | PFAM: protein of unknown function DUF167; KEGG: cph:Cpha266_2081 protein of unknown function DUF167; Belongs to the UPF0235 family. | 3-deoxy-D-manno-octulosonate cytidylyltransferase; Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. | 0.773 |
Clim_2042 | Clim_1937 | Clim_2042 | Clim_1937 | KEGG: cph:Cpha266_2083 citrate synthase; TIGRFAM: citrate synthase I; PFAM: Citrate synthase; Belongs to the citrate synthase family. | PFAM: glutamine amidotransferase class-II; glutamate synthase alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase; KEGG: cph:Cpha266_0628 glutamate synthase (NADH) large subunit. | 0.902 |
Clim_2042 | Clim_2040 | Clim_2042 | Clim_2040 | KEGG: cph:Cpha266_2083 citrate synthase; TIGRFAM: citrate synthase I; PFAM: Citrate synthase; Belongs to the citrate synthase family. | PFAM: protein of unknown function DUF167; KEGG: cph:Cpha266_2081 protein of unknown function DUF167; Belongs to the UPF0235 family. | 0.682 |
Clim_2042 | dtd | Clim_2042 | Clim_2039 | KEGG: cph:Cpha266_2083 citrate synthase; TIGRFAM: citrate synthase I; PFAM: Citrate synthase; Belongs to the citrate synthase family. | D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | 0.684 |
Clim_2042 | gatC | Clim_2042 | Clim_2041 | KEGG: cph:Cpha266_2083 citrate synthase; TIGRFAM: citrate synthase I; PFAM: Citrate synthase; Belongs to the citrate synthase family. | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.711 |
Clim_2042 | kdsB | Clim_2042 | Clim_2038 | KEGG: cph:Cpha266_2083 citrate synthase; TIGRFAM: citrate synthase I; PFAM: Citrate synthase; Belongs to the citrate synthase family. | 3-deoxy-D-manno-octulosonate cytidylyltransferase; Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. | 0.678 |
aspS | gatA | Clim_1519 | Clim_0332 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | glutamyl-tRNA(Gln) amidotransferase, A subunit; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). | 0.742 |
aspS | gatB | Clim_1519 | Clim_2287 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | glutamyl-tRNA(Gln) amidotransferase, B subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.978 |
aspS | gatC | Clim_1519 | Clim_2041 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.803 |
dapA | gatC | Clim_0622 | Clim_2041 | Dihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.731 |
dtd | Clim_2040 | Clim_2039 | Clim_2040 | D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | PFAM: protein of unknown function DUF167; KEGG: cph:Cpha266_2081 protein of unknown function DUF167; Belongs to the UPF0235 family. | 0.777 |
dtd | Clim_2042 | Clim_2039 | Clim_2042 | D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | KEGG: cph:Cpha266_2083 citrate synthase; TIGRFAM: citrate synthase I; PFAM: Citrate synthase; Belongs to the citrate synthase family. | 0.684 |
dtd | gatC | Clim_2039 | Clim_2041 | D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.763 |