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Daes_0381 Daes_0381 Daes_0382 Daes_0382 Daes_1288 Daes_1288 nuoB nuoB Daes_1290 Daes_1290 nuoD nuoD nuoH nuoH Daes_1293 Daes_1293 Daes_1294 Daes_1294 nuoK nuoK Daes_1299 Daes_1299 Daes_1482 Daes_1482 Daes_2065 Daes_2065 Daes_2066 Daes_2066 Daes_2067 Daes_2067 atpC atpC atpD atpD atpG atpG atpA atpA atpH atpH atpF atpF atpF-2 atpF-2 atpE atpE atpB atpB
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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:
Daes_0381KEGG: dma:DMR_28310 cytochrome d ubiquinol oxidase subunit II; TIGRFAM: cytochrome d ubiquinol oxidase, subunit II; PFAM: cytochrome bd ubiquinol oxidase subunit II. (350 aa)
Daes_0382PFAM: cytochrome bd ubiquinol oxidase subunit I; KEGG: dvm:DvMF_2473 cytochrome bd ubiquinol oxidase subunit I. (440 aa)
Daes_1288NADH-ubiquinone/plastoquinone oxidoreductase chain 3; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. (125 aa)
nuoBNADH-quinone oxidoreductase, B subunit; 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. (181 aa)
Daes_1290PFAM: NADH dehydrogenase (ubiquinone) 30 kDa subunit; KEGG: dvm:DvMF_1595 NADH dehydrogenase (ubiquinone) 30 kDa subunit. (175 aa)
nuoDNADH dehydrogenase (quinone); 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 49 kDa subunit family. (390 aa)
nuoHNADH dehydrogenase (quinone); 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. (324 aa)
Daes_1293KEGG: dsa:Desal_1494 4Fe-4S ferredoxin iron-sulfur binding domain protein. (195 aa)
Daes_1294NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. (169 aa)
nuoKNADH-ubiquinone oxidoreductase chain 4L; 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)
Daes_1299KEGG: dsa:Desal_1500 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (510 aa)
Daes_1482KEGG: dsa:Desal_2248 inorganic diphosphatase; PFAM: DHHA2 domain protein; phosphoesterase RecJ domain protein. (306 aa)
Daes_2065KEGG: dba:Dbac_3064 fumarate reductase iron-sulfur subunit; TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein. (245 aa)
Daes_2066TIGRFAM: succinate dehydrogenase or fumarate reductase, flavoprotein subunit; KEGG: dsa:Desal_0721 fumarate reductase flavoprotein subunit; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein. (611 aa)
Daes_2067PFAM: succinate dehydrogenase cytochrome b subunit; KEGG: dba:Dbac_3066 fumarate reductase respiratory complex transmembrane subunit. (216 aa)
atpCATP synthase F1, epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. (140 aa)
atpDATP synthase F1, 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. (465 aa)
atpGATP synthase F1, gamma subunit; 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. (291 aa)
atpAATP synthase F1, alpha subunit; 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. (502 aa)
atpHATP synthase F1, delta subunit; 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 F0, B subunit; 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. (190 aa)
atpF-2H+transporting two-sector ATPase B/B' subunit; 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. (140 aa)
atpEATP synthase F0, C subunit; 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. (102 aa)
atpBATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (240 aa)
Your Current Organism:
Pseudodesulfovibrio aespoeensis
NCBI taxonomy Id: 643562
Other names: Desulfovibrio aespoeensis Aspo-2, Desulfovibrio aespoeensis DSM 10631, P. aespoeensis Aspo-2, Pseudodesulfovibrio aespoeensis Aspo-2, Pseudodesulfovibrio aespoeensis DSM 10631
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