| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADO47164.1 | ADO48674.1 | Entcl_0892 | Entcl_2423 | AMP-dependent synthetase and ligase; Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1; In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. | Phenylacetic acid degradation protein paaN; KEGG: enc:ECL_02154 bifunctional aldehyde dehydrogenase/enoyl-CoA hydratase; TIGRFAM: phenylacetic acid degradation protein paaN; PFAM: MaoC domain protein dehydratase; Aldehyde Dehydrogenase. | 0.585 |
| ADO47164.1 | ADO48687.1 | Entcl_0892 | Entcl_2436 | AMP-dependent synthetase and ligase; Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1; In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. | KEGG: ent:Ent638_2136 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; Pyruvate-flavodoxin oxidoreductase, EKR domain; thiamine pyrophosphate TPP-binding domain-containing protein. | 0.570 |
| ADO47164.1 | ADO49454.1 | Entcl_0892 | Entcl_3208 | AMP-dependent synthetase and ligase; Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1; In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. | Amino acid adenylation domain protein; KEGG: kpe:KPK_3973 enterobactin synthase subunit F; TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; phosphopantetheine-binding; Thioesterase. | 0.710 |
| ADO47164.1 | ADO49546.1 | Entcl_0892 | Entcl_3301 | AMP-dependent synthetase and ligase; Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1; In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. | PFAM: short-chain dehydrogenase/reductase SDR; KEGG: ssn:SSON_0482 short chain dehydrogenase. | 0.543 |
| ADO47164.1 | fadB | Entcl_0892 | Entcl_4192 | AMP-dependent synthetase and ligase; Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1; In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. | Fatty oxidation complex, alpha subunit FadB; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. | 0.779 |
| ADO48674.1 | ADO47164.1 | Entcl_2423 | Entcl_0892 | Phenylacetic acid degradation protein paaN; KEGG: enc:ECL_02154 bifunctional aldehyde dehydrogenase/enoyl-CoA hydratase; TIGRFAM: phenylacetic acid degradation protein paaN; PFAM: MaoC domain protein dehydratase; Aldehyde Dehydrogenase. | AMP-dependent synthetase and ligase; Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1; In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. | 0.585 |
| ADO48674.1 | ADO48687.1 | Entcl_2423 | Entcl_2436 | Phenylacetic acid degradation protein paaN; KEGG: enc:ECL_02154 bifunctional aldehyde dehydrogenase/enoyl-CoA hydratase; TIGRFAM: phenylacetic acid degradation protein paaN; PFAM: MaoC domain protein dehydratase; Aldehyde Dehydrogenase. | KEGG: ent:Ent638_2136 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; Pyruvate-flavodoxin oxidoreductase, EKR domain; thiamine pyrophosphate TPP-binding domain-containing protein. | 0.685 |
| ADO48674.1 | ADO49454.1 | Entcl_2423 | Entcl_3208 | Phenylacetic acid degradation protein paaN; KEGG: enc:ECL_02154 bifunctional aldehyde dehydrogenase/enoyl-CoA hydratase; TIGRFAM: phenylacetic acid degradation protein paaN; PFAM: MaoC domain protein dehydratase; Aldehyde Dehydrogenase. | Amino acid adenylation domain protein; KEGG: kpe:KPK_3973 enterobactin synthase subunit F; TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; phosphopantetheine-binding; Thioesterase. | 0.410 |
| ADO48674.1 | ADO49546.1 | Entcl_2423 | Entcl_3301 | Phenylacetic acid degradation protein paaN; KEGG: enc:ECL_02154 bifunctional aldehyde dehydrogenase/enoyl-CoA hydratase; TIGRFAM: phenylacetic acid degradation protein paaN; PFAM: MaoC domain protein dehydratase; Aldehyde Dehydrogenase. | PFAM: short-chain dehydrogenase/reductase SDR; KEGG: ssn:SSON_0482 short chain dehydrogenase. | 0.506 |
| ADO48674.1 | fadB | Entcl_2423 | Entcl_4192 | Phenylacetic acid degradation protein paaN; KEGG: enc:ECL_02154 bifunctional aldehyde dehydrogenase/enoyl-CoA hydratase; TIGRFAM: phenylacetic acid degradation protein paaN; PFAM: MaoC domain protein dehydratase; Aldehyde Dehydrogenase. | Fatty oxidation complex, alpha subunit FadB; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. | 0.830 |
| ADO48674.1 | polA | Entcl_2423 | Entcl_4391 | Phenylacetic acid degradation protein paaN; KEGG: enc:ECL_02154 bifunctional aldehyde dehydrogenase/enoyl-CoA hydratase; TIGRFAM: phenylacetic acid degradation protein paaN; PFAM: MaoC domain protein dehydratase; Aldehyde Dehydrogenase. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.585 |
| ADO48687.1 | ADO47164.1 | Entcl_2436 | Entcl_0892 | KEGG: ent:Ent638_2136 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; Pyruvate-flavodoxin oxidoreductase, EKR domain; thiamine pyrophosphate TPP-binding domain-containing protein. | AMP-dependent synthetase and ligase; Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1; In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. | 0.570 |
| ADO48687.1 | ADO48674.1 | Entcl_2436 | Entcl_2423 | KEGG: ent:Ent638_2136 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; Pyruvate-flavodoxin oxidoreductase, EKR domain; thiamine pyrophosphate TPP-binding domain-containing protein. | Phenylacetic acid degradation protein paaN; KEGG: enc:ECL_02154 bifunctional aldehyde dehydrogenase/enoyl-CoA hydratase; TIGRFAM: phenylacetic acid degradation protein paaN; PFAM: MaoC domain protein dehydratase; Aldehyde Dehydrogenase. | 0.685 |
| ADO48687.1 | ADO49546.1 | Entcl_2436 | Entcl_3301 | KEGG: ent:Ent638_2136 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; Pyruvate-flavodoxin oxidoreductase, EKR domain; thiamine pyrophosphate TPP-binding domain-containing protein. | PFAM: short-chain dehydrogenase/reductase SDR; KEGG: ssn:SSON_0482 short chain dehydrogenase. | 0.445 |
| ADO48687.1 | ADO49547.1 | Entcl_2436 | Entcl_3302 | KEGG: ent:Ent638_2136 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; Pyruvate-flavodoxin oxidoreductase, EKR domain; thiamine pyrophosphate TPP-binding domain-containing protein. | PFAM: Thioredoxin domain-containing protein; KEGG: enc:ECL_01259 putative thioredoxin-like protein. | 0.460 |
| ADO48687.1 | fadB | Entcl_2436 | Entcl_4192 | KEGG: ent:Ent638_2136 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; Pyruvate-flavodoxin oxidoreductase, EKR domain; thiamine pyrophosphate TPP-binding domain-containing protein. | Fatty oxidation complex, alpha subunit FadB; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. | 0.710 |
| ADO48687.1 | polA | Entcl_2436 | Entcl_4391 | KEGG: ent:Ent638_2136 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; Pyruvate-flavodoxin oxidoreductase, EKR domain; thiamine pyrophosphate TPP-binding domain-containing protein. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.469 |
| ADO49454.1 | ADO47164.1 | Entcl_3208 | Entcl_0892 | Amino acid adenylation domain protein; KEGG: kpe:KPK_3973 enterobactin synthase subunit F; TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; phosphopantetheine-binding; Thioesterase. | AMP-dependent synthetase and ligase; Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1; In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. | 0.710 |
| ADO49454.1 | ADO48674.1 | Entcl_3208 | Entcl_2423 | Amino acid adenylation domain protein; KEGG: kpe:KPK_3973 enterobactin synthase subunit F; TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; phosphopantetheine-binding; Thioesterase. | Phenylacetic acid degradation protein paaN; KEGG: enc:ECL_02154 bifunctional aldehyde dehydrogenase/enoyl-CoA hydratase; TIGRFAM: phenylacetic acid degradation protein paaN; PFAM: MaoC domain protein dehydratase; Aldehyde Dehydrogenase. | 0.410 |
| ADO49454.1 | ADO49546.1 | Entcl_3208 | Entcl_3301 | Amino acid adenylation domain protein; KEGG: kpe:KPK_3973 enterobactin synthase subunit F; TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; phosphopantetheine-binding; Thioesterase. | PFAM: short-chain dehydrogenase/reductase SDR; KEGG: ssn:SSON_0482 short chain dehydrogenase. | 0.460 |