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KMT57153.1 KMT57153.1 KMT57306.1 KMT57306.1 KMT56703.1 KMT56703.1 KMT56705.1 KMT56705.1 KMT56706.1 KMT56706.1 KMT56707.1 KMT56707.1 KMT56709.1 KMT56709.1 KMT56710.1 KMT56710.1 KMT56470.1 KMT56470.1 KMT56492.1 KMT56492.1 KMT56493.1 KMT56493.1 KMT56498.1 KMT56498.1 KMT56049.1 KMT56049.1 KMT56253.1 KMT56253.1 KMT56351.1 KMT56351.1 KMT56352.1 KMT56352.1 KMT55756.1 KMT55756.1 KMT55160.1 KMT55160.1 KMT55161.1 KMT55161.1 KMT55356.1 KMT55356.1 KMT54901.1 KMT54901.1 nuoA nuoA nuoB nuoB KMT53717.1 KMT53717.1 KMT53718.1 KMT53718.1 KMT53719.1 KMT53719.1 nuoH nuoH nuoI nuoI KMT53722.1 KMT53722.1 nuoK nuoK KMT53724.1 KMT53724.1 KMT53725.1 KMT53725.1 KMT53817.1 KMT53817.1 KMT53113.1 KMT53113.1 sdhA sdhA sdhB sdhB KMT53174.1 KMT53174.1 KMT52696.1 KMT52696.1 KMT52706.1 KMT52706.1 KMT52719.1 KMT52719.1 KMT52458.1 KMT52458.1 KMT52322.1 KMT52322.1
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:
KMT57153.1NAD(FAD)-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (102 aa)
KMT57306.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0312 family. (196 aa)
KMT56703.1Cytochrome Cbb3; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (325 aa)
KMT56705.1Cbb3-type cytochrome c oxidase subunit II; CcoO; FixO; Derived by automated computational analysis using gene prediction method: Protein Homology. (202 aa)
KMT56706.1Cbb3-type cytochrome c oxidase subunit I; CcoN; FixN; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. (480 aa)
KMT56707.1Cytochrome Cbb3; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (304 aa)
KMT56709.1Cbb3-type cytochrome c oxidase subunit II; CcoO; FixO; Derived by automated computational analysis using gene prediction method: Protein Homology. (202 aa)
KMT56710.1Cbb3-type cytochrome c oxidase subunit I; CcoN; FixN; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. (474 aa)
KMT56470.1Cytochrome; Derived by automated computational analysis using gene prediction method: Protein Homology. (99 aa)
KMT56492.1Cytochrome oxidase subunit I; 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. (529 aa)
KMT56493.1Cytochrome B559 subunit alpha; 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). (375 aa)
KMT56498.1Alcohol dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (432 aa)
KMT56049.12-amino-4-hydroxy-6- hydroxymethyldihydropteridine pyrophosphokinase; Derived by automated computational analysis using gene prediction method: Protein Homology. (172 aa)
KMT56253.1Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (83 aa)
KMT56351.1Cytochrome o ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. (672 aa)
KMT56352.1Ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (313 aa)
KMT55756.1Derived by automated computational analysis using gene prediction method: Protein Homology. (137 aa)
KMT55160.1Derived by automated computational analysis using gene prediction method: Protein Homology. (258 aa)
KMT55161.1Cytochrome B; 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. (403 aa)
KMT55356.12-amino-4-hydroxy-6- hydroxymethyldihydropteridine pyrophosphokinase; Derived by automated computational analysis using gene prediction method: Protein Homology. (162 aa)
KMT54901.1Derived by automated computational analysis using gene prediction method: Protein Homology. (153 aa)
nuoANADH-quinone 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 ubiquinone. 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. (137 aa)
nuoBNADH 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 ubiquinone. 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. (224 aa)
KMT53717.1NADH dehydrogenase; Catalyzes the transfer of electrons from NADH to quinone; Derived by automated computational analysis using gene prediction method: Protein Homology. (165 aa)
KMT53718.1NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. (451 aa)
KMT53719.1NADH dehydrogenase; 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. Belongs to the complex I 75 kDa subunit family. (904 aa)
nuoHNADH:ubiquinone oxidoreductase; 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 ubiquinone. 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. This subunit may bind ubiquinone. (335 aa)
nuoINADH 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 ubiquinone. 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. (182 aa)
KMT53722.1NADH dehydrogenase; 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. (167 aa)
nuoKNADH-quinone oxidoreductase subunit K; 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 ubiquinone. 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 4L family. (102 aa)
KMT53724.1NADH-quinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. (617 aa)
KMT53725.1NADH:ubiquinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (510 aa)
KMT53817.1Alcohol dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (704 aa)
KMT53113.1Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (124 aa)
sdhAPart of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (590 aa)
sdhBPart of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; the catalytic subunits are similar to fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (234 aa)
KMT53174.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (602 aa)
KMT52696.1Protease; Derived by automated computational analysis using gene prediction method: Protein Homology. (296 aa)
KMT52706.1Nitric oxide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. (473 aa)
KMT52719.1Cytochrome Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. (484 aa)
KMT52458.1Derived by automated computational analysis using gene prediction method: Protein Homology. (268 aa)
KMT52322.1Alcohol dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (446 aa)
Your Current Organism:
Pseudomonas sp. KG01
NCBI taxonomy Id: 1674920
Other names: P. sp. KG01
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