STRINGSTRING
KML35995.1 KML35995.1 KML35736.1 KML35736.1 KML35735.1 KML35735.1 KML35734.1 KML35734.1 KML35999.1 KML35999.1 KML35997.1 KML35997.1 KML35996.1 KML35996.1 KML35994.1 KML35994.1 KML36271.1 KML36271.1 KML36489.1 KML36489.1 KML39826.1 KML39826.1 KML39825.1 KML39825.1 KML45240.1 KML45240.1 KML46305.1 KML46305.1 nuoN nuoN KML46457.1 KML46457.1 KML46456.1 KML46456.1 KML46454.1 KML46454.1 KML46450.1 KML46450.1 nqo6 nqo6 nuoA nuoA KML46680.1 KML46680.1 KML46675.1 KML46675.1
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
KML35995.1Quinol oxidase subunit 1; 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 are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (622 aa)
KML35736.1Quinol oxidase subunit 2; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. (330 aa)
KML35735.1Quinol oxidase subunit 1; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. (658 aa)
KML35734.1Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. (201 aa)
KML35999.1Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (155 aa)
KML35997.1Cytochrome B6; Derived by automated computational analysis using gene prediction method: Protein Homology. (111 aa)
KML35996.1Cytochrome B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (209 aa)
KML35994.1Cytochrome B; 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). (358 aa)
KML36271.1Subunit D of antiporter complex involved in resistance to high concentrations of Na+, K+, Li+ and/or alkali; contains an oxidoreductase domain; catalyzes the transfer of electrons from NADH to ubiquinone; Derived by automated computational analysis using gene prediction method: Protein Homology. (497 aa)
KML36489.1Subunit D of antiporter complex involved in resistance to high concentrations of Na+, K+, Li+ and/or alkali; contains an oxidoreductase domain; catalyzes the transfer of electrons from NADH to ubiquinone; Derived by automated computational analysis using gene prediction method: Protein Homology. (496 aa)
KML39826.1Cytochrome C oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (488 aa)
KML39825.1Cytochrome c oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (183 aa)
KML45240.1(2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (110 aa)
KML46305.1Cytochrome c oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (123 aa)
nuoNNADH:ubiquinone oxidoreductase subunit N; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 2 family. (506 aa)
KML46457.1NADH:ubiquinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (505 aa)
KML46456.1NADH:ubiquinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. (622 aa)
KML46454.1NADH:ubiquinone oxidoreductase subunit J; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (173 aa)
KML46450.1NADH-quinone oxidoreductase subunit C; Derived by automated computational analysis using gene prediction method: Protein Homology. (427 aa)
nqo6NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (170 aa)
nuoANADH:ubiquinone oxidoreductase subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 3 family. (124 aa)
KML46680.1Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (413 aa)
KML46675.1Cytochrome B5; Derived by automated computational analysis using gene prediction method: Protein Homology. (158 aa)
Your Current Organism:
Bacillus firmus
NCBI taxonomy Id: 1399
Other names: ATCC 14575, B. firmus, BCRC 11730, Bacillaceae bacterium HQ2, Bacillus sp. JP44SK20, Bacillus sp. LK28, Bacillus sp. NCIM 2264, Bacillus sp. NCIM 2462, CCM 2213, CCRC 11730, CCRC:11730, CCUG 7418, CIP 52.70, DSM 12, IAM 12464, IFO 15306, JCM 2512, LMG 7125, LMG:7125, NBRC 15306, NCAIM B.01087, NCCB 48015, NCIB 9366, NCIMB 9366, NCTC 10335, NRRL B-14307, NRRL NRS-613, VKM B-498
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