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Daro_0174 Daro_0174 Daro_0445 Daro_0445 Daro_0564 Daro_0564 Daro_0566 Daro_0566 Daro_0567 Daro_0567 Daro_0568 Daro_0568 Daro_0576 Daro_0576 Daro_0624 Daro_0624 Daro_0713 Daro_0713 Daro_0714 Daro_0714 Daro_0715 Daro_0715 Daro_0716 Daro_0716 Daro_0809 Daro_0809 Daro_0810 Daro_0810 Daro_0811 Daro_0811 nuoA nuoA nuoB nuoB nuoC nuoC nuoD nuoD Daro_0953 Daro_0953 Daro_0954 Daro_0954 Daro_0955 Daro_0955 nuoH nuoH nuoI nuoI Daro_0958 Daro_0958 nuoK nuoK Daro_0960 Daro_0960 Daro_0961 Daro_0961 nuoN nuoN Daro_0979 Daro_0979 Daro_0980 Daro_0980 Daro_1065 Daro_1065 Daro_1173 Daro_1173 Daro_1462 Daro_1462 ctaB ctaB Daro_1464 Daro_1464 Daro_1465 Daro_1465 Daro_1466 Daro_1466 Daro_1467 Daro_1467 Daro_1468 Daro_1468 Daro_1470 Daro_1470 Daro_1471 Daro_1471 Daro_1472 Daro_1472 Daro_1576 Daro_1576 Daro_1577 Daro_1577 Daro_1578 Daro_1578 Daro_1914 Daro_1914 Daro_1945 Daro_1945 acpP acpP Daro_2433 Daro_2433 Daro_2492 Daro_2492 Daro_3138 Daro_3138 Daro_3719 Daro_3719 Daro_3721 Daro_3721 Daro_3724 Daro_3724 Daro_3774 Daro_3774 Daro_3859 Daro_3859 Daro_3877 Daro_3877 Daro_4134 Daro_4134 Daro_4136 Daro_4136 Daro_4137 Daro_4137 Daro_4140 Daro_4140 Daro_4169 Daro_4169 Daro_4171 Daro_4171
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:
Daro_0174Amino acid adenylation; Belongs to the ATP-dependent AMP-binding enzyme family. (1332 aa)
Daro_0445Putative denitrification protein NorE. (199 aa)
Daro_0564NADH dehydrogenase subunit M. (481 aa)
Daro_0566NADH-Ubiquinone oxidoreductase (complex I), chain 5/L, N-terminal:NADH/Ubiquinone/plastoquinone (complex I). (508 aa)
Daro_0567NADH dehydrogenase subunit M. (503 aa)
Daro_0568NADH dehydrogenase subunit M. (485 aa)
Daro_0576Protein of unknown function DUF59; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. (363 aa)
Daro_0624Cytochrome c, class I. (211 aa)
Daro_0713Cytochrome c oxidase cbb3-type, subunit I; Belongs to the heme-copper respiratory oxidase family. (475 aa)
Daro_0714Cytochrome C oxidase, mono-heme subunit/FixO. (211 aa)
Daro_0715Cbb3-type cytochrome oxidase component. (58 aa)
Daro_0716Cytochrome c oxidase cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (299 aa)
Daro_0809Ubiquinol-cytochrome c reductase, iron-sulfur subunit; 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. (198 aa)
Daro_0810Cytochrome b/b6, N-terminal:Cytochrome b/b6, C-terminal; 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. (433 aa)
Daro_0811Cytochrome c1. (239 aa)
nuoANADH dehydrogenase 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. (124 aa)
nuoBNADH dehydrogenase subunit B; 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 (By similarity). (158 aa)
nuoCNADH dehydrogenase subunit C; 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 30 kDa subunit family. (201 aa)
nuoDNADH dehydrogenase subunit D; 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. (417 aa)
Daro_0953NADH dehydrogenase subunit E. (157 aa)
Daro_0954NADH dehydrogenase subunit F; 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. (442 aa)
Daro_0955NADH dehydrogenase subunit G; 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. (777 aa)
nuoHNADH dehydrogenase subunit H; 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. (349 aa)
nuoINADH dehydrogenase subunit I; 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. (162 aa)
Daro_0958NADH dehydrogenase 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. (198 aa)
nuoKNADH dehydrogenase 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. (103 aa)
Daro_0960NADH dehydrogenase subunit L. (682 aa)
Daro_0961NADH dehydrogenase subunit M. (494 aa)
nuoNNADH dehydrogenase 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 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 2 family. (494 aa)
Daro_0979NAD(P)-dependent nickel-iron dehydrogenase flavin-containing subunit. (632 aa)
Daro_0980Ferredoxin. (235 aa)
Daro_1065Putative denitrification protein NorE. (201 aa)
Daro_1173Phosphopantetheine-binding protein. (79 aa)
Daro_1462Cytochrome oxidase assembly. (348 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. (298 aa)
Daro_1464Probable transmembrane protein. (192 aa)
Daro_1465Surfeit locus 1. (228 aa)
Daro_1466Conserved hypothetical protein. (69 aa)
Daro_1467Cytochrome c oxidase, subunit III. (290 aa)
Daro_1468Cytochrome c oxidase assembly protein CtaG/Cox11. (203 aa)
Daro_1470Cytochrome 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. (531 aa)
Daro_1471Cytochrome c oxidase subunit 2; 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). (401 aa)
Daro_1472Electron transport protein SCO1/SenC. (192 aa)
Daro_1576Hypothetical protein. (156 aa)
Daro_1577Electron transport protein SCO1/SenC. (200 aa)
Daro_1578Protein of unknown function DUF461. (160 aa)
Daro_1914Alpha/beta hydrolase fold protein. (268 aa)
Daro_1945Putative acyl-carrier-protein. (86 aa)
acpPAcyl carrier protein (ACP); Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family. (78 aa)
Daro_2433Conserved hypothetical protein. (90 aa)
Daro_2492Cytochrome c, class I. (698 aa)
Daro_3138Cytochrome c, class I. (205 aa)
Daro_3719Peptidase M16, C-terminal:Peptidase M16, N-terminal; Belongs to the peptidase M16 family. (452 aa)
Daro_3721Peptidase M16, C-terminal:Peptidase M16, N-terminal. (429 aa)
Daro_37244Fe-4S ferredoxin, iron-sulfur binding protein. (85 aa)
Daro_3774Thiol-disulfide isomerase-like protein; Similar to thioredoxins. (173 aa)
Daro_3859Probable cytochrome c5. (206 aa)
Daro_3877Cytochrome c, class I. (147 aa)
Daro_4134NAD-dependent epimerase/dehydratase:3-beta hydroxysteroid dehydrogenase/isomerase:dTDP-4-dehydrorhamnose reductase:NmrA-like protein. (320 aa)
Daro_4136Conserved hypothetical protein. (75 aa)
Daro_4137Alpha/beta hydrolase fold protein. (268 aa)
Daro_4140Protein of unknown function DUF185. (386 aa)
Daro_4169Phosphopantetheine-binding protein. (79 aa)
Daro_4171Acyl carrier protein. (94 aa)
Your Current Organism:
Dechloromonas aromatica
NCBI taxonomy Id: 159087
Other names: D. aromatica RCB, Dechloromonas aromatica RCB, Dechloromonas aromatica str. RCB, Dechloromonas sp. RCB
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