| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| azo1348 | ccoG | azo1348 | azo1345 | Probable transmemebrane Protein, 38% Idneity to TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. TMHMM2 reporting 1 TMH present. | Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...] | 0.823 |
| azo1348 | ccoH | azo1348 | azo1346 | Probable transmemebrane Protein, 38% Idneity to TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. TMHMM2 reporting 1 TMH present. | Conserved hypothetical membrane protein. Homology to ebA5136 Azoarcus sp. EbN1 of 51% (gnl|keqq|eba:ebA5136(KEGG)). Has PF05751, FixH;IPR008620; This family consists of several Rhizobium FixH like proteins. It has been suggested that suggested that the four proteins FixG, FixH, FixI, and FixS may participate in a membrane-bound complex coupling the FixI cation pump with a redox process catalysed by FixG. No signal peptide predicted. 1 TMHs; Conserved hypothetical protein. | 0.890 |
| azo1348 | ccoN | azo1348 | azo1341 | Probable transmemebrane Protein, 38% Idneity to TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. TMHMM2 reporting 1 TMH present. | Probable cytochrome c oxidase, cbb3-type, subunit I. Homology to ccoN of R. capsulatus of 62% (sprot|COX1_RHOCA). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoN: cytochrome c oxidase cbb3-type Pfam: cytochrome c and quinol oxidase polyppeptide no signal peptide 12 TMHs; Hig [...] | 0.471 |
| azo1348 | ccoO | azo1348 | azo1342 | Probable transmemebrane Protein, 38% Idneity to TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. TMHMM2 reporting 1 TMH present. | Probable cytochrome c oxidase, cbb3-type, subunit II Homology to ccoO of P. stutzeri of 58% (trembl|Q8KS21). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoO: cytochrome c oxidase cbb3-type, subunit II Pfam: Cytochrome c oxidase, mono-heme subunit no signal peptide probable 1 [...] | 0.486 |
| azo1348 | ccoP | azo1348 | azo1344 | Probable transmemebrane Protein, 38% Idneity to TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. TMHMM2 reporting 1 TMH present. | Probable cytochrome c oxidase, cbb3-type,subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.665 |
| azo1348 | ccoQ | azo1348 | azo1343 | Probable transmemebrane Protein, 38% Idneity to TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. TMHMM2 reporting 1 TMH present. | Cbb3-type cytochrome oxidase, subunit ccoQ, 44% Identity to TrEMBL;Q8D9I3, Q7MKV5,Q9KS21. Has PF05545,Cbb3-type cytochrome oxidase component FixQ; IPR008621;This family consists of several Cbb3-type cytochrome oxidase components (FixQ/CcoQ). FixQ is found in nitrogen fixing bacteria. Since nitrogen fixation is an energy-consuming process, effective symbioses depend on operation of a respiratory chain with a high affinity for O2, closely coupled to ATP production. This requirement is fulfilled by a special three-subunit terminal oxidase (cytochrome terminal oxidase cbb3), which was firs [...] | 0.649 |
| azo1348 | ccoS | azo1348 | azo1340 | Probable transmemebrane Protein, 38% Idneity to TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. TMHMM2 reporting 1 TMH present. | Conserved hypothetical cytochrome oxidase maturation protein. Homology to cco of P.Putida of 42% (gnl|keqq|ppu:PP4262(KEGG)). Pfam: Cytochrome oxidase maturation protein cbb3-type. Genes encoding a cytochrome cbb3 oxidase were initially designated fixNOQP (ccoNOQP),the ccoNOQP operon is always found close to a second gene cluster, known as fixGHIS (ccoGHIS) whose expression is necessary for the assembly of a functional cbb3 oxidase. On the basis of their derived amino acid sequences each of the four proteins encoded by the ccoGHIS operon are thought to be membrane-bound. It has been su [...] | 0.451 |
| azo3085 | ccoO | azo3085 | azo1342 | Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein. | Probable cytochrome c oxidase, cbb3-type, subunit II Homology to ccoO of P. stutzeri of 58% (trembl|Q8KS21). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoO: cytochrome c oxidase cbb3-type, subunit II Pfam: Cytochrome c oxidase, mono-heme subunit no signal peptide probable 1 [...] | 0.971 |
| azo3085 | ccoP | azo3085 | azo1344 | Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein. | Probable cytochrome c oxidase, cbb3-type,subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.639 |
| azo3085 | ccoQ | azo3085 | azo1343 | Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein. | Cbb3-type cytochrome oxidase, subunit ccoQ, 44% Identity to TrEMBL;Q8D9I3, Q7MKV5,Q9KS21. Has PF05545,Cbb3-type cytochrome oxidase component FixQ; IPR008621;This family consists of several Cbb3-type cytochrome oxidase components (FixQ/CcoQ). FixQ is found in nitrogen fixing bacteria. Since nitrogen fixation is an energy-consuming process, effective symbioses depend on operation of a respiratory chain with a high affinity for O2, closely coupled to ATP production. This requirement is fulfilled by a special three-subunit terminal oxidase (cytochrome terminal oxidase cbb3), which was firs [...] | 0.887 |
| azo3085 | coxB | azo3085 | azo3304 | Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein. | Conserved hypothetical cytochrome c oxidase,subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.937 |
| ccoG | azo1348 | azo1345 | azo1348 | Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...] | Probable transmemebrane Protein, 38% Idneity to TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. TMHMM2 reporting 1 TMH present. | 0.823 |
| ccoG | ccoH | azo1345 | azo1346 | Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...] | Conserved hypothetical membrane protein. Homology to ebA5136 Azoarcus sp. EbN1 of 51% (gnl|keqq|eba:ebA5136(KEGG)). Has PF05751, FixH;IPR008620; This family consists of several Rhizobium FixH like proteins. It has been suggested that suggested that the four proteins FixG, FixH, FixI, and FixS may participate in a membrane-bound complex coupling the FixI cation pump with a redox process catalysed by FixG. No signal peptide predicted. 1 TMHs; Conserved hypothetical protein. | 0.944 |
| ccoG | ccoN | azo1345 | azo1341 | Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...] | Probable cytochrome c oxidase, cbb3-type, subunit I. Homology to ccoN of R. capsulatus of 62% (sprot|COX1_RHOCA). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoN: cytochrome c oxidase cbb3-type Pfam: cytochrome c and quinol oxidase polyppeptide no signal peptide 12 TMHs; Hig [...] | 0.954 |
| ccoG | ccoO | azo1345 | azo1342 | Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...] | Probable cytochrome c oxidase, cbb3-type, subunit II Homology to ccoO of P. stutzeri of 58% (trembl|Q8KS21). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoO: cytochrome c oxidase cbb3-type, subunit II Pfam: Cytochrome c oxidase, mono-heme subunit no signal peptide probable 1 [...] | 0.971 |
| ccoG | ccoP | azo1345 | azo1344 | Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...] | Probable cytochrome c oxidase, cbb3-type,subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.973 |
| ccoG | ccoQ | azo1345 | azo1343 | Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...] | Cbb3-type cytochrome oxidase, subunit ccoQ, 44% Identity to TrEMBL;Q8D9I3, Q7MKV5,Q9KS21. Has PF05545,Cbb3-type cytochrome oxidase component FixQ; IPR008621;This family consists of several Cbb3-type cytochrome oxidase components (FixQ/CcoQ). FixQ is found in nitrogen fixing bacteria. Since nitrogen fixation is an energy-consuming process, effective symbioses depend on operation of a respiratory chain with a high affinity for O2, closely coupled to ATP production. This requirement is fulfilled by a special three-subunit terminal oxidase (cytochrome terminal oxidase cbb3), which was firs [...] | 0.757 |
| ccoG | ccoS | azo1345 | azo1340 | Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...] | Conserved hypothetical cytochrome oxidase maturation protein. Homology to cco of P.Putida of 42% (gnl|keqq|ppu:PP4262(KEGG)). Pfam: Cytochrome oxidase maturation protein cbb3-type. Genes encoding a cytochrome cbb3 oxidase were initially designated fixNOQP (ccoNOQP),the ccoNOQP operon is always found close to a second gene cluster, known as fixGHIS (ccoGHIS) whose expression is necessary for the assembly of a functional cbb3 oxidase. On the basis of their derived amino acid sequences each of the four proteins encoded by the ccoGHIS operon are thought to be membrane-bound. It has been su [...] | 0.706 |
| ccoH | azo1348 | azo1346 | azo1348 | Conserved hypothetical membrane protein. Homology to ebA5136 Azoarcus sp. EbN1 of 51% (gnl|keqq|eba:ebA5136(KEGG)). Has PF05751, FixH;IPR008620; This family consists of several Rhizobium FixH like proteins. It has been suggested that suggested that the four proteins FixG, FixH, FixI, and FixS may participate in a membrane-bound complex coupling the FixI cation pump with a redox process catalysed by FixG. No signal peptide predicted. 1 TMHs; Conserved hypothetical protein. | Probable transmemebrane Protein, 38% Idneity to TrEMBL;Q8XZW3 Signal P reporting Signal peptide present. TMHMM2 reporting 1 TMH present. | 0.890 |
| ccoH | ccoG | azo1346 | azo1345 | Conserved hypothetical membrane protein. Homology to ebA5136 Azoarcus sp. EbN1 of 51% (gnl|keqq|eba:ebA5136(KEGG)). Has PF05751, FixH;IPR008620; This family consists of several Rhizobium FixH like proteins. It has been suggested that suggested that the four proteins FixG, FixH, FixI, and FixS may participate in a membrane-bound complex coupling the FixI cation pump with a redox process catalysed by FixG. No signal peptide predicted. 1 TMHs; Conserved hypothetical protein. | Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...] | 0.944 |
