| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| aas | atpE | azo0150 | azo0154 | AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. 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 MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...] | Probable ATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.479 |
| aas | azo0147 | azo0150 | azo0147 | AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. 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 MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...] | Conserved hypothetical membrane protein. Homology to RS05051 of Ralstonia solanacearum of 45% (trembl|Q8Y1A4(SRS)). TMHMM2 reporting the presence of 26 TMH's. Signal P reporting Signal Peptide present. Coils2 program reporting presence of Coiled coil; Conserved hypothetical protein. | 0.748 |
| aas | azo0148 | azo0150 | azo0148 | AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. 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 MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...] | Putative acyltransferase family protein; Similar to the Aas bifunctional protein [includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-gpe acyltransferase); acyl-acyl carrier protein synthetase (acyl-acp synthetase)].Plays a role in lysophospholipid acylation. 25% Acyltransferase.IPR000873; AMP-bind. Pfam:PF01553; Acyltransferase; 1.PF00501; AMP-binding; 1. TMhelix:10; Function unclear. | 0.860 |
| aas | azo0152 | azo0150 | azo0152 | AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. 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 MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...] | Conserved hypothetical membrane protein. Homology to BB4612 of Bordetella bronchiseptica of 37% (trembl|Q7WEM2(SRS)). No domains predicted. signal peptide 3 TMHs; Conserved hypothetical protein. | 0.457 |
| aas | smtB | azo0150 | azo0151 | AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. 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 MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...] | Putative transcriptional repressor,; High confidence in function and specificity. | 0.662 |
| aas | uxuA | azo0150 | azo0149 | AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. 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 MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...] | Putative mannonate dehydratase; tremblnew|AAR36422:35% identity, 46% similarity EMBL:AE017218; AAR36422.1; TIGR:GSU3030; This Fe2+-requiring enzyme plays a role in D-glucuronate catabolism in Escherichia coli. Mannonate dehydratase converts D-mannonate to 2-dehydro-3-deoxy-D-gluconate. An apparent equivalog is found in a glucuronate utilization operon in Bacillus stearothermophilus T-6. Interpro:IPR004628;Man_dehyd SignalP predicted signal peptide present. No. of transmembrane helices: 1 (TMHMM predicted) pyrC_dimer: dihydroorotase homodimeric; Specificity unclear. | 0.836 |
| atpB | atpE | azo0153 | azo0154 | Probable ATP synthase A chain; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Probable ATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.999 |
| atpB | atpH | azo0153 | azo0156 | Probable ATP synthase A chain; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Putative ATP synthase delta chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | 0.999 |
| atpB | azo0152 | azo0153 | azo0152 | Probable ATP synthase A chain; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Conserved hypothetical membrane protein. Homology to BB4612 of Bordetella bronchiseptica of 37% (trembl|Q7WEM2(SRS)). No domains predicted. signal peptide 3 TMHs; Conserved hypothetical protein. | 0.997 |
| atpB | smtB | azo0153 | azo0151 | Probable ATP synthase A chain; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Putative transcriptional repressor,; High confidence in function and specificity. | 0.510 |
| atpE | aas | azo0154 | azo0150 | Probable ATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. 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 MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...] | 0.479 |
| atpE | atpB | azo0154 | azo0153 | Probable ATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Probable ATP synthase A chain; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | 0.999 |
| atpE | atpH | azo0154 | azo0156 | Probable ATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Putative ATP synthase delta chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | 0.999 |
| atpE | azo0148 | azo0154 | azo0148 | Probable ATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Putative acyltransferase family protein; Similar to the Aas bifunctional protein [includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-gpe acyltransferase); acyl-acyl carrier protein synthetase (acyl-acp synthetase)].Plays a role in lysophospholipid acylation. 25% Acyltransferase.IPR000873; AMP-bind. Pfam:PF01553; Acyltransferase; 1.PF00501; AMP-binding; 1. TMhelix:10; Function unclear. | 0.451 |
| atpE | azo0152 | azo0154 | azo0152 | Probable ATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Conserved hypothetical membrane protein. Homology to BB4612 of Bordetella bronchiseptica of 37% (trembl|Q7WEM2(SRS)). No domains predicted. signal peptide 3 TMHs; Conserved hypothetical protein. | 0.988 |
| atpE | smtB | azo0154 | azo0151 | Probable ATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Putative transcriptional repressor,; High confidence in function and specificity. | 0.408 |
| atpH | atpB | azo0156 | azo0153 | Putative ATP synthase delta chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | Probable ATP synthase A chain; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | 0.999 |
| atpH | atpE | azo0156 | azo0154 | Putative ATP synthase delta chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | Probable ATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.999 |
| atpH | azo0152 | azo0156 | azo0152 | Putative ATP synthase delta chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | Conserved hypothetical membrane protein. Homology to BB4612 of Bordetella bronchiseptica of 37% (trembl|Q7WEM2(SRS)). No domains predicted. signal peptide 3 TMHs; Conserved hypothetical protein. | 0.986 |
| atpH | smtB | azo0156 | azo0151 | Putative ATP synthase delta chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. | Putative transcriptional repressor,; High confidence in function and specificity. | 0.452 |