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ppk ppk ndhC ndhC ndhK ndhK ndhJ ndhJ AII42334.1 AII42334.1 ndhN ndhN ndhB ndhB AII42651.1 AII42651.1 AII42652.1 AII42652.1 AII42653.1 AII42653.1 AII42654.1 AII42654.1 ctaB ctaB AII42732.1 AII42732.1 AII42761.1 AII42761.1 AII42827.1 AII42827.1 AII42828.1 AII42828.1 AII42985.1 AII42985.1 AII43875.1 AII43875.1 ndhL ndhL AII43920.1 AII43920.1 AII43921.1 AII43921.1 AII43922.1 AII43922.1 AII44253.1 AII44253.1 sdhA sdhA AII44255.1 AII44255.1 atpD atpD atpC atpC atpG atpG atpA atpA atpH atpH atpF atpF atpG-2 atpG-2 atpE atpE atpB atpB ndhM ndhM AII44621.1 AII44621.1 ndhD ndhD ndhE ndhE AII44631.1 AII44631.1 ndhI ndhI ndhA ndhA ndhH ndhH
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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
protein homology
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ppkPolyphosphate kinase; Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Belongs to the polyphosphate kinase 1 (PPK1) family. (711 aa)
ndhCNADPH-quinone oxidoreductase; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (120 aa)
ndhKNADH dehydrogenase subunit B; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration; Belongs to the complex I 20 kDa subunit family. (245 aa)
ndhJNADH dehydrogenase subunit J; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (188 aa)
AII42334.1N-acetylglucosamine-1-phosphate uridyltransferase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (505 aa)
ndhNNAD(P)H-quinone oxidoreductase subunit N; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (153 aa)
ndhBOxidoreductase; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (523 aa)
AII42651.1Cytochrome B6; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (208 aa)
AII42652.1Cytochrome C 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. (557 aa)
AII42653.1Cytochrome 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). (292 aa)
AII42654.1Cytochrome C oxidase assembly protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (308 aa)
ctaBProtoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. (312 aa)
AII42732.1Inorganic pyrophosphatase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (195 aa)
AII42761.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (132 aa)
AII42827.1Oxidoreductase; Catalyzes the transfer of electrons from NADH to ubiquinone; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (614 aa)
AII42828.1NAD(P)H-quinone oxidoreductase subunit D4; Catalyzes the transfer of electrons from NADH to ubiquinone; NdhD4 is possibly involved in a constitutive CO(2)-uptake system; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (496 aa)
AII42985.1Polyphosphate kinase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (315 aa)
AII43875.1NAD(P)H-quinone oxidoreductase subunit 4; Shuttles electrons from NAD(P)H, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain; subunit D, with NdhB and NdhF are core membrane components; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (523 aa)
ndhLHypothetical protein; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (83 aa)
AII43920.1Cytochrome 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). (311 aa)
AII43921.1Cytochrome C oxidase subunit I; Derived by automated computational analysis using gene prediction method: GeneMarkS+; Belongs to the heme-copper respiratory oxidase family. (562 aa)
AII43922.1Cytochrome B6; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (198 aa)
AII44253.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (214 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: GeneMarkS+. (638 aa)
AII44255.1Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (242 aa)
atpDF0F1 ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. (487 aa)
atpCF0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. (138 aa)
atpGF0F1 ATP synthase subunit gamma; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. (326 aa)
atpAF0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. (506 aa)
atpHF0F1 ATP synthase subunit delta; 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. (182 aa)
atpFHypothetical protein; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family. (171 aa)
atpG-2F0F1 ATP synthase subunit B; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria. Belongs to the ATPase B chain family. (154 aa)
atpEF0F1 ATP synthase subunit C; 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. (82 aa)
atpBF0F1 ATP synthase subunit A; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family. (241 aa)
ndhMNAD(P)H-quinone oxidoreductase subunit M; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (115 aa)
AII44621.1Oxidoreductase; Catalyzes the transfer of electrons from NADH to ubiquinone; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (669 aa)
ndhDNAD(P)H-quinone oxidoreductase subunit 4; NDH-1 shuttles electrons from NAD(P)H, 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 plastoquinone. 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 4 family. (544 aa)
ndhENADH:ubiquinone oxidoreductase subunit K; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (109 aa)
AII44631.1NADH: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. Belongs to the complex I subunit 6 family. (200 aa)
ndhINADH dehydrogenase subunit I; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient; Belongs to the complex I 23 kDa subunit family. (215 aa)
ndhANADPH-quinone oxidoreductase; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. (373 aa)
ndhHNADPH-quinone oxidoreductase; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (394 aa)
Your Current Organism:
Synechococcus sp. KORDI100
NCBI taxonomy Id: 1280380
Other names: S. sp. KORDI-100, Synechococcus sp. KORDI-100
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