STRINGSTRING
CEW89_07420 CEW89_07420 CEW89_07430 CEW89_07430 nuoN nuoN CEW89_07440 CEW89_07440 CEW89_07445 CEW89_07445 nuoK nuoK CEW89_07460 CEW89_07460 nuoI nuoI nuoH nuoH CEW89_07480 CEW89_07480 CEW89_07485 CEW89_07485 CEW89_07490 CEW89_07490 CEW89_07495 CEW89_07495 CEW89_07500 CEW89_07500 CEW89_07505 CEW89_07505 CEW89_07510 CEW89_07510 CEW89_07515 CEW89_07515 GCA_001550095_00153 GCA_001550095_00153 CEW89_07525 CEW89_07525 nuoD nuoD CEW89_07535 CEW89_07535 nuoC nuoC nuoB nuoB nuoA nuoA CEW89_00335 CEW89_00335 ctaD ctaD CEW89_17225 CEW89_17225 fdhD fdhD CEW89_17215 CEW89_17215 CEW89_17210 CEW89_17210 CEW89_17205 CEW89_17205 CEW89_17200 CEW89_17200 CEW89_05720 CEW89_05720 ctaA ctaA CEW89_14860 CEW89_14860 coxB coxB ctaB ctaB ctaG ctaG CEW89_17685 CEW89_17685 CEW89_17690 CEW89_17690 CEW89_17700 CEW89_17700 CEW89_17705 CEW89_17705 CEW89_17710 CEW89_17710 CEW89_00875 CEW89_00875 CEW89_00870 CEW89_00870 CEW89_00865 CEW89_00865 CEW89_00860 CEW89_00860 CEW89_00855 CEW89_00855 CEW89_00850 CEW89_00850 CEW89_00845 CEW89_00845 CEW89_00840 CEW89_00840 CEW89_00835 CEW89_00835 CEW89_00830 CEW89_00830 CEW89_00825 CEW89_00825 CEW89_00820 CEW89_00820 CEW89_00815 CEW89_00815 CEW89_00810 CEW89_00810 ctaB-2 ctaB-2 cyoA cyoA cyoB cyoB cyoC cyoC cyoD cyoD CEW89_00570 CEW89_00570 GCA_001550095_03575 GCA_001550095_03575 GCA_001550095_03577 GCA_001550095_03577 CEW89_10700 CEW89_10700 petA petA CEW89_12405 CEW89_12405 CEW89_12410 CEW89_12410 CEW89_12530 CEW89_12530
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:
CEW89_07420Unannotated protein. (553 aa)
CEW89_07430Unannotated protein. (250 aa)
nuoNUnannotated protein; 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. (478 aa)
CEW89_07440Unannotated protein. (510 aa)
CEW89_07445Unannotated protein. (697 aa)
nuoKUnannotated protein; 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. (101 aa)
CEW89_07460Unannotated protein; 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. (204 aa)
nuoIUnannotated protein; 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. (163 aa)
nuoHUnannotated protein; 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. (345 aa)
CEW89_07480Unannotated protein. (140 aa)
CEW89_07485Unannotated protein; 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. (672 aa)
CEW89_07490Unannotated protein. (132 aa)
CEW89_07495Unannotated protein. (136 aa)
CEW89_07500Unannotated protein. (166 aa)
CEW89_07505Unannotated protein. (137 aa)
CEW89_07510Unannotated protein; 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. (432 aa)
CEW89_07515Unannotated protein. (73 aa)
GCA_001550095_00153Unannotated protein. (222 aa)
CEW89_07525Unannotated protein. (385 aa)
nuoDUnannotated protein; 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. (413 aa)
CEW89_07535Unannotated protein. (298 aa)
nuoCUnannotated protein; 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. (200 aa)
nuoBUnannotated protein; 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. (177 aa)
nuoAUnannotated protein; 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. (121 aa)
CEW89_00335Unannotated protein. (169 aa)
ctaDUnannotated protein; 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. (563 aa)
CEW89_17225Unannotated protein. (67 aa)
fdhDUnannotated protein; Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH. Belongs to the FdhD family. (243 aa)
CEW89_17215Unannotated protein. (974 aa)
CEW89_17210Unannotated protein. (508 aa)
CEW89_17205Unannotated protein. (166 aa)
CEW89_17200Unannotated protein; Belongs to the LysR transcriptional regulatory family. (295 aa)
CEW89_05720Unannotated protein. (128 aa)
ctaAUnannotated protein; Catalyzes the oxidation of the C8 methyl side group on heme O porphyrin ring into a formyl group; Belongs to the COX15/CtaA family. Type 2 subfamily. (380 aa)
CEW89_14860Unannotated protein. (109 aa)
coxBUnannotated protein; 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). (291 aa)
ctaBUnannotated protein; 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; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. (316 aa)
ctaGUnannotated protein; Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I; Belongs to the COX11/CtaG family. (193 aa)
CEW89_17685Unannotated protein. (267 aa)
CEW89_17690Unannotated protein. (221 aa)
CEW89_17700Unannotated protein; Belongs to the peptidase M16 family. (419 aa)
CEW89_17705Unannotated protein. (196 aa)
CEW89_17710Unannotated protein. (470 aa)
CEW89_00875Unannotated protein; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. (317 aa)
CEW89_00870Unannotated protein. (179 aa)
CEW89_00865Unannotated protein. (87 aa)
CEW89_00860Unannotated protein. (112 aa)
CEW89_00855Unannotated protein. (83 aa)
CEW89_00850Unannotated protein. (237 aa)
CEW89_00845Unannotated protein. (119 aa)
CEW89_00840Unannotated protein. (1041 aa)
CEW89_00835Unannotated protein. (305 aa)
CEW89_00830Unannotated protein; Belongs to the complex I 20 kDa subunit family. (229 aa)
CEW89_00825Unannotated protein. (185 aa)
CEW89_00820Unannotated protein; Belongs to the complex I 49 kDa subunit family. (392 aa)
CEW89_00815Unannotated protein. (602 aa)
CEW89_00810Unannotated protein. (164 aa)
ctaB-2Unannotated protein; 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; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. (318 aa)
cyoAUnannotated protein. (365 aa)
cyoBUnannotated protein; Belongs to the heme-copper respiratory oxidase family. (665 aa)
cyoCUnannotated protein. (201 aa)
cyoDUnannotated protein. (138 aa)
CEW89_00570Unannotated protein. (235 aa)
GCA_001550095_03575Unannotated protein. (169 aa)
GCA_001550095_03577Unannotated protein. (563 aa)
CEW89_10700Unannotated protein. (172 aa)
petAUnannotated protein; 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. (187 aa)
CEW89_12405Unannotated protein; 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. (468 aa)
CEW89_12410Unannotated protein. (272 aa)
CEW89_12530Unannotated protein. (328 aa)
Your Current Organism:
Celeribacter ethanolicus
NCBI taxonomy Id: 1758178
Other names: C. ethanolicus, CGMCC 1.15406, Celeribacter ethanolicus Jian et al. 2016, Celeribacter sp. NH195, JCM 31095, strain NH195
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