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atpC atpC atpA atpA atpD atpD atpF atpF atpG atpG atpH atpH atpI atpI ndhA ndhA ndhI ndhI ndhG ndhG ndhE ndhE ndhD ndhD alr0751 alr0751 hoxF hoxF hoxU hoxU ndhF ndhF ndhD-2 ndhD-2 all0945 all0945 all0948 all0948 all0949 all0949 coxB coxB coxA coxA coxC coxC all1126 all1126 all1127 all1127 all1553 all1553 all1732 all1732 alr2191 alr2191 coxB-2 coxB-2 coxA-2 coxA-2 coxC-2 coxC-2 coxB-3 coxB-3 coxA-3 coxA-3 coxC-3 coxC-3 all2964 all2964 all2970 all2970 all3341 all3341 ndhH ndhH ppa ppa alr3593 alr3593 ndhJ ndhJ ndhK ndhK ndhC ndhC ndhF-2 ndhF-2 ndhD-3 ndhD-3 all4023 all4023 all4024 all4024 ndhF-3 ndhF-3 ndhD-4 ndhD-4 alr4216 alr4216 ictA ictA ndhB ndhB atpE atpE atpB atpB ndhD-5 ndhD-5 alr5211 alr5211
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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
Your Input:
atpCATP 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. (315 aa)
atpAATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit; Belongs to the ATPase alpha/beta chains family. (506 aa)
atpDATP 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; Belongs to the ATPase delta chain family. (183 aa)
atpFATP synthase subunit b; 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. (187 aa)
atpGATP synthase subunit b; 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. (163 aa)
atpHATP 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. (81 aa)
atpIATP synthase subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (251 aa)
ndhANADH dehydrogenase subunit 1; 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. (372 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. (194 aa)
ndhGNADH dehydrogenase subunit 6; 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 (By similarity); Belongs to the complex I subunit 6 family. (202 aa)
ndhENADH dehydrogenase subunit 4L; 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. (101 aa)
ndhDNADH dehydrogenase 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. (538 aa)
alr0751NADH dehydrogenase I chain E; ORF_ID:alr0751. (164 aa)
hoxFHydrogenase subunit; ORF_ID:alr0752; hoxF gene product. (544 aa)
hoxUHydrogenase chain U; ORF_ID:alr0762; hoxU gene product. (238 aa)
ndhFNADH dehydrogenase subunit 5; ORF_ID:alr0869. (618 aa)
ndhD-2NADH dehydrogenase subunit 4; ORF_ID:alr0870. (500 aa)
all0945Succinate dehydrogenase iron-sulfur protein subunit; ORF_ID:all0945; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (333 aa)
all0948Heme O synthase; 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. (318 aa)
all0949ORF_ID:all0949; hypothetical protein. (333 aa)
coxBCytochrome 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). (355 aa)
coxACytochrome 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. (575 aa)
coxCCytochrome c oxidase subunit III; ORF_ID:alr0952. (207 aa)
all1126NADH dehydrogenase; ORF_ID:all1126. (456 aa)
all1127NADH dehydrogenase; ORF_ID:all1127. (453 aa)
all1553NADH dehydrogenase; ORF_ID:all1553. (439 aa)
all1732NAD(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. (118 aa)
alr2191ORF_ID:alr2191; hypothetical protein. (305 aa)
coxB-2Cytochrome 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). (327 aa)
coxA-2Cytochrome 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. (559 aa)
coxC-2Cytochrome c oxidase subunit III; ORF_ID:alr2516. (197 aa)
coxB-3Cytochrome 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). (304 aa)
coxA-3Cytochrome 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. (555 aa)
coxC-3Cytochrome c oxidase subunit III; ORF_ID:alr2734. (200 aa)
all2964ORF_ID:all2964; probable NADH dehydrogenase. (442 aa)
all2970Succinate dehydrogenase flavoprotein; ORF_ID:all2970. (575 aa)
all3341Heterodisulfide reductase, subunit B; ORF_ID:all3341. (301 aa)
ndhHNADH dehydrogenase subunit 7; 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)
ppaInorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions; Belongs to the PPase family. (169 aa)
alr3593Polyphosphate 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. (736 aa)
ndhJNADH dehydrogenase chain 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. (175 aa)
ndhKNADH dehydrogenase chain 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; Belongs to the complex I 20 kDa subunit family. (245 aa)
ndhCNADH dehydrogenase subunit 3; 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)
ndhF-2NADH dehydrogenase subunit 5; ORF_ID:alr3956. (696 aa)
ndhD-3NADH dehydrogenase 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 (By similarity); Belongs to the complex I subunit 4 family. (525 aa)
all4023Cytochrome D ubiquinol oxidase chain II; ORF_ID:all4023. (346 aa)
all4024Cytochrome D ubiquinol oxidase chain I; ORF_ID:all4024; Belongs to the cytochrome ubiquinol oxidase subunit 1 family. (480 aa)
ndhF-3NADH dehydrogenase subunit 5; ORF_ID:alr4156. (620 aa)
ndhD-4NADH dehydrogenase subunit 4; ORF_ID:alr4157. (500 aa)
alr4216NAD(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. (162 aa)
ictAInorganic carbon transport; 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. (70 aa)
ndhBNADH dehydrogenase subunit 2; 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. (520 aa)
atpEATP synthase epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. (137 aa)
atpBATP synthase beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. (482 aa)
ndhD-5NADH dehydrogenase 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 (By similarity); Belongs to the complex I subunit 4 family. (560 aa)
alr5211ORF_ID:alr5211; probable NADH dehydrogenase. (470 aa)
Your Current Organism:
Nostoc sp. PCC7120
NCBI taxonomy Id: 103690
Other names: Anabaena sp. (ATCC 27893), Anabaena sp. (PCC 7120), Anabaena sp. DCC D0672, Anabaena sp. PCC 7120, Anabaena sp. SAG 25.82, Anabaena sp. UTEX B 2576, Anabaena variabilis UTCC 387, N. sp. PCC 7120, Nostoc muscorum ISU, Nostoc sp. AKM24, Nostoc sp. ATCC 27347, Nostoc sp. ATCC 72893, Nostoc sp. DSM 107007, Nostoc sp. Ind43, Nostoc sp. PCC 7120, Nostoc sp. SAG 25.82
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