| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| accC1 | amiD | azo0862 | azo1956 | Probable biotin carboxylase (a subunit of acetyl-coa carboxylase); This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. | Amidase; Putative amidase amiD; Family membership; Belongs to the amidase family. | 0.632 |
| accC1 | azo0044 | azo0862 | azo0044 | Probable biotin carboxylase (a subunit of acetyl-coa carboxylase); This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. | Conserved hypothetical urea amidolyase-related protein. Homology to ybgK of E. coli of 36% (sprot|YBGK_ECOLI). InterPro: DUF183 (IPR003778) Uncharacterized domain in proteins of unknown function. This domain is found in a multifunctional enzyme, urea amidolyase, from yeast. Pfam: DFU182, uncharcterized ACR,COG1984 no signal peptide no TMHs; Function unclear. | 0.937 |
| accC1 | tms | azo0862 | azo1955 | Probable biotin carboxylase (a subunit of acetyl-coa carboxylase); This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. | Indoleacetamide hydrolase (EC 3.5.1.-) (IAH) (Indole-3-acetamide hydrolase). Hydrolyzes indole-3-acetamide (IAM) into indole-3- acetic acid (IAA); Family membership; Belongs to the amidase family. | 0.797 |
| amiD | accC1 | azo1956 | azo0862 | Amidase; Putative amidase amiD; Family membership; Belongs to the amidase family. | Probable biotin carboxylase (a subunit of acetyl-coa carboxylase); This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. | 0.632 |
| amiD | aspS | azo1956 | azo3239 | Amidase; Putative amidase amiD; Family membership; Belongs to the amidase family. | AspS protein; 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. | 0.794 |
| amiD | azo0044 | azo1956 | azo0044 | Amidase; Putative amidase amiD; Family membership; Belongs to the amidase family. | Conserved hypothetical urea amidolyase-related protein. Homology to ybgK of E. coli of 36% (sprot|YBGK_ECOLI). InterPro: DUF183 (IPR003778) Uncharacterized domain in proteins of unknown function. This domain is found in a multifunctional enzyme, urea amidolyase, from yeast. Pfam: DFU182, uncharcterized ACR,COG1984 no signal peptide no TMHs; Function unclear. | 0.654 |
| amiD | gatB | azo1956 | azo0170 | Amidase; Putative amidase amiD; Family membership; Belongs to the amidase family. | glutamyl-tRNA(GLN) amidotransferase subunit B; 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. | 0.993 |
| amiD | gatC | azo1956 | azo0173 | Amidase; Putative amidase amiD; Family membership; Belongs to the amidase family. | glutamyl-tRNA(GLN) amidotransferase subunit C; 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. | 0.989 |
| amiD | glnS | azo1956 | azo0836 | Amidase; Putative amidase amiD; Family membership; Belongs to the amidase family. | Glutaminyl-tRNA synthetase (EC 6.1.1.18) (Glutamine--tRNA ligase) (GlnRS). glnS: glutaminyl-tRNA synthetase; High confidence in function and specificity. | 0.831 |
| amiD | gltX2 | azo1956 | azo1479 | Amidase; Putative amidase amiD; Family membership; Belongs to the amidase family. | Glutamate-tRNA ligase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.826 |
| amiD | gluQ | azo1956 | azo0745 | Amidase; Putative amidase amiD; Family membership; Belongs to the amidase family. | Glutamate-tRNA ligase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | 0.772 |
| amiD | mhpC | azo1956 | azo1957 | Amidase; Putative amidase amiD; Family membership; Belongs to the amidase family. | 2-hydroxy-6-ketonona-2,4-dienedioic acid hydrolase; TREMBLNEW:47357: 69% identity, 80% similarity. 2-hydroxy-6-oxo-6-phenylhexa-24-dienoate hydrolase. The alpha/beta hydrolase fold [1] is common to a number of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function. The core of each enzyme is an alpha/beta-sheet (rather than a barrel), containing 8 strands connected by helices Pfam: Ndr family. TIGR00148: conserved hypothetical protein; High confidence in function and specificity. | 0.815 |
| amiD | tms | azo1956 | azo1955 | Amidase; Putative amidase amiD; Family membership; Belongs to the amidase family. | Indoleacetamide hydrolase (EC 3.5.1.-) (IAH) (Indole-3-acetamide hydrolase). Hydrolyzes indole-3-acetamide (IAM) into indole-3- acetic acid (IAA); Family membership; Belongs to the amidase family. | 0.715 |
| aspS | amiD | azo3239 | azo1956 | AspS protein; 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. | Amidase; Putative amidase amiD; Family membership; Belongs to the amidase family. | 0.794 |
| aspS | gatB | azo3239 | azo0170 | AspS protein; 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 subunit B; 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. | 0.998 |
| aspS | gatC | azo3239 | azo0173 | AspS protein; 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 subunit C; 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. | 0.964 |
| aspS | glnS | azo3239 | azo0836 | AspS protein; 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. | Glutaminyl-tRNA synthetase (EC 6.1.1.18) (Glutamine--tRNA ligase) (GlnRS). glnS: glutaminyl-tRNA synthetase; High confidence in function and specificity. | 0.719 |
| aspS | gltX2 | azo3239 | azo1479 | AspS protein; 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. | Glutamate-tRNA ligase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.601 |
| aspS | gluQ | azo3239 | azo0745 | AspS protein; 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. | Glutamate-tRNA ligase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | 0.463 |
| aspS | tms | azo3239 | azo1955 | AspS protein; 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. | Indoleacetamide hydrolase (EC 3.5.1.-) (IAH) (Indole-3-acetamide hydrolase). Hydrolyzes indole-3-acetamide (IAM) into indole-3- acetic acid (IAA); Family membership; Belongs to the amidase family. | 0.800 |