| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 [...] | 0.964 |
| 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 [...] | 0.969 |
| 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. | 0.970 |
| 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 [...] | 0.761 |
| ccoN | ccoG | azo1341 | azo1345 | 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 [...] | 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 [...] | 0.964 |
| ccoN | ccoO | azo1341 | azo1342 | 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 [...] | 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 [...] | 0.999 |
| ccoN | ccoP | azo1341 | azo1344 | 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 [...] | Probable cytochrome c oxidase, cbb3-type,subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.999 |
| ccoN | ccoQ | azo1341 | azo1343 | 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 [...] | 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 [...] | 0.998 |
| ccoN | coxB | azo1341 | azo3304 | 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 [...] | 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). | 0.989 |
| ccoN | coxC | azo1341 | azo3299 | 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 [...] | Cytochrome c oxidase polypeptide III Subunits I II and III form the functional core of the enzyme complex. InterPro: Cytochrome c oxidase subunit III; High confidence in function and specificity. | 0.935 |
| ccoN | petA1 | azo1341 | azo0960 | 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 [...] | Probable ubiquinol-cytochrome c reductase iron-sulfur protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.872 |
| ccoN | petA2 | azo1341 | azo1235 | 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 [...] | Probable ubiquinol-cytochrome C reductase iron-sulfur protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.871 |
| ccoN | petB | azo1341 | azo0961 | 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 [...] | Ubiquinol-cytochrome c reductase cytochrome b protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.935 |
| ccoN | petC | azo1341 | azo0962 | 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 [...] | Conserved hypothetical ubiquinol-cytochrome c reductase cytochrome c1 protein. Homology to petC of R. solanacearum of 52% (trembl|Q8XVA4). Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. c1 functions as an electron donor to cytochrome c. InterPro: Cytochrome c1 (IPR002326) Pfam: Cytochrome_c1 signal peptide 1 TMH; Conserved hypothetical protein. | 0.921 |
| ccoO | ccoG | azo1342 | azo1345 | 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 [...] | 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 [...] | 0.969 |
| ccoO | ccoN | azo1342 | azo1341 | 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 [...] | 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 [...] | 0.999 |
| ccoO | ccoP | azo1342 | azo1344 | 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 [...] | Probable cytochrome c oxidase, cbb3-type,subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.999 |
| ccoO | ccoQ | azo1342 | azo1343 | 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 [...] | 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 [...] | 0.998 |
| ccoO | coxB | azo1342 | azo3304 | 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 [...] | 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). | 0.990 |
| ccoO | coxC | azo1342 | azo3299 | 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 [...] | Cytochrome c oxidase polypeptide III Subunits I II and III form the functional core of the enzyme complex. InterPro: Cytochrome c oxidase subunit III; High confidence in function and specificity. | 0.922 |