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SKC86286.1 SKC86286.1 SKC86290.1 SKC86290.1 ctaB ctaB SKC86296.1 SKC86296.1 SKC86299.1 SKC86299.1 SKC38648.1 SKC38648.1 SKC38756.1 SKC38756.1 SKC39005.1 SKC39005.1 atpD atpD SKC43703.1 SKC43703.1 SKC43717.1 SKC43717.1 SKC43722.1 SKC43722.1 SKC43748.1 SKC43748.1 nuoA nuoA nuoB nuoB nuoC nuoC nuoD nuoD SKC44393.1 SKC44393.1 SKC44401.1 SKC44401.1 SKC44405.1 SKC44405.1 nuoH nuoH nuoI nuoI SKC44456.1 SKC44456.1 nuoK nuoK SKC44481.1 SKC44481.1 SKC44491.1 SKC44491.1 nuoN nuoN SKC45094.1 SKC45094.1 SKC45108.1 SKC45108.1 SKC45398.1 SKC45398.1 SKC46282.1 SKC46282.1 SKC47954.1 SKC47954.1 SKC48770.1 SKC48770.1 SKC48778.1 SKC48778.1 SKC48785.1 SKC48785.1 nuoA-2 nuoA-2 nuoB-2 nuoB-2 nuoC-2 nuoC-2 nuoD-2 nuoD-2 SKC55812.1 SKC55812.1 SKC56128.1 SKC56128.1 SKC56141.1 SKC56141.1 SKC58028.1 SKC58028.1 SKC86302.1 SKC86302.1 SKC87430.1 SKC87430.1 SKC87862.1 SKC87862.1 SKC88526.1 SKC88526.1 SKC89200.1 SKC89200.1 SKC89204.1 SKC89204.1 atpH atpH SKC89602.1 SKC89602.1 atpF atpF atpE atpE atpB atpB SKC76219.1 SKC76219.1 rbfA rbfA SKC74251.1 SKC74251.1 SKC73248.1 SKC73248.1 SKC61258.1 SKC61258.1 ppa ppa atpA atpA atpG atpG nuoH-2 nuoH-2 SKC78448.1 SKC78448.1 SKC78454.1 SKC78454.1 nuoK-2 nuoK-2 SKC78466.1 SKC78466.1 SKC78470.1 SKC78470.1 nuoN-2 nuoN-2 SKC81699.1 SKC81699.1 ppk ppk SKC82630.1 SKC82630.1 SKC82852.1 SKC82852.1 SKC83614.1 SKC83614.1 ppk-2 ppk-2 nuoN-3 nuoN-3 SKC85523.1 SKC85523.1 SKC85527.1 SKC85527.1 nuoK-3 nuoK-3 SKC85534.1 SKC85534.1 nuoI-2 nuoI-2 nuoH-3 nuoH-3 SKC85544.1 SKC85544.1 SKC85549.1 SKC85549.1 SKC85551.1 SKC85551.1 nuoD-3 nuoD-3 nuoB-3 nuoB-3 nuoA-3 nuoA-3 SKC85741.1 SKC85741.1 SKC86063.1 SKC86063.1 SKC86113.1 SKC86113.1 SKC86275.1 SKC86275.1
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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
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SKC86286.1Cytochrome c oxidase subunit 3. (248 aa)
SKC86290.1Cytochrome c oxidase subunit 3. (194 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)
SKC86296.1Cytochrome c oxidase assembly protein subunit 15. (336 aa)
SKC86299.1Cytochrome c oxidase subunit 1; Belongs to the heme-copper respiratory oxidase family. (630 aa)
SKC38648.1Zinc protease. (943 aa)
SKC38756.1Predicted Zn-dependent peptidase. (419 aa)
SKC39005.1F-type H+-transporting ATPase subunit epsilon. (81 aa)
atpDF-type H+-transporting ATPase 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. (502 aa)
SKC43703.1Cytochrome c oxidase cbb3-type subunit 3. (317 aa)
SKC43717.1Hypothetical protein. (64 aa)
SKC43722.1Cytochrome c oxidase cbb3-type subunit I/II; Belongs to the heme-copper respiratory oxidase family. (711 aa)
SKC43748.1Cytochrome oxidase maturation protein, cbb3-type. (67 aa)
nuoANADH-quinone oxidoreductase 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 a menaquinone. 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. (123 aa)
nuoBNADH-quinone oxidoreductase subunit B; 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 a menaquinone. 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. (186 aa)
nuoCNADH-quinone oxidoreductase 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 a menaquinone. 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. (166 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 a menaquinone. 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. (406 aa)
SKC44393.1NADH-quinone oxidoreductase subunit E. (182 aa)
SKC44401.1NADH-quinone oxidoreductase 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. (450 aa)
SKC44405.1NADH-quinone oxidoreductase subunit G. (334 aa)
nuoHNADH-quinone oxidoreductase 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. (348 aa)
nuoINADH-quinone oxidoreductase 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. (188 aa)
SKC44456.1NADH 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. (165 aa)
nuoKNADH-quinone oxidoreductase 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 a menaquinone. 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)
SKC44481.1NADH-quinone oxidoreductase subunit L. (637 aa)
SKC44491.1NADH-quinone oxidoreductase subunit M. (490 aa)
nuoNNADH-quinone oxidoreductase 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 a menaquinone. 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. (459 aa)
SKC45094.1NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus. (622 aa)
SKC45108.1Hypothetical protein; Belongs to the UPF0753 family. (847 aa)
SKC45398.1Predicted Zn-dependent peptidase. (422 aa)
SKC46282.1(2Fe-2S) ferredoxin. (259 aa)
SKC47954.1NADH dehydrogenase. (442 aa)
SKC48770.1Succinate dehydrogenase / fumarate reductase iron-sulfur subunit. (256 aa)
SKC48778.1Succinate dehydrogenase subunit A. (640 aa)
SKC48785.1Succinate dehydrogenase / fumarate reductase cytochrome b subunit. (224 aa)
nuoA-2NADH-quinone oxidoreductase 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 a menaquinone. 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. (168 aa)
nuoB-2NADH dehydrogenase subunit B; 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 a menaquinone. 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. (184 aa)
nuoC-2NADH 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 a menaquinone. 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. (160 aa)
nuoD-2NADH 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 a menaquinone. 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. (406 aa)
SKC55812.14Fe-4S dicluster domain-containing protein. (118 aa)
SKC56128.1Cytochrome d ubiquinol oxidase subunit II. (344 aa)
SKC56141.1Cytochrome d ubiquinol oxidase subunit I. (472 aa)
SKC58028.1Hypothetical protein. (513 aa)
SKC86302.1Cytochrome 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). (355 aa)
SKC87430.1Starch-binding associating with outer membrane. (565 aa)
SKC87862.1(2Fe-2S) ferredoxin. (93 aa)
SKC88526.1Starch-binding associating with outer membrane. (499 aa)
SKC89200.1Predicted Zn-dependent peptidase. (446 aa)
SKC89204.1Predicted Zn-dependent peptidase. (453 aa)
atpHF-type H+-transporting ATPase 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. (186 aa)
SKC89602.1Starch-binding associating with outer membrane. (564 aa)
atpFF-type H+-transporting ATPase subunit b; 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. (164 aa)
atpEF-type H+-transporting ATPase 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)
atpBF-type H+-transporting ATPase 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. (349 aa)
SKC76219.1Predicted Zn-dependent peptidase. (412 aa)
rbfARibosome-binding factor A; One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA. (125 aa)
SKC74251.1Hypothetical protein. (315 aa)
SKC73248.1WbqC-like protein family protein. (208 aa)
SKC61258.1Starch-binding associating with outer membrane. (504 aa)
ppaInorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (178 aa)
atpAF-type H+-transporting ATPase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. (526 aa)
atpGATP synthase F1 subcomplex 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. (296 aa)
nuoH-2NADH-quinone oxidoreductase 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. (362 aa)
SKC78448.1Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase subunit (chain I). (231 aa)
SKC78454.1NADH-quinone 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. (170 aa)
nuoK-2NADH-quinone oxidoreductase 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 a menaquinone. 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)
SKC78466.1NADH-quinone oxidoreductase subunit L. (625 aa)
SKC78470.1NADH-quinone oxidoreductase subunit M. (537 aa)
nuoN-2NADH-quinone oxidoreductase 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 a menaquinone. 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. (503 aa)
SKC81699.1Ca2+-transporting ATPase. (858 aa)
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. (708 aa)
SKC82630.1Polyphosphate:nucleotide phosphotransferase, PPK2 family. (312 aa)
SKC82852.1Zinc protease. (945 aa)
SKC83614.1Ca2+-transporting ATPase. (833 aa)
ppk-2Polyphosphate 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. (691 aa)
nuoN-3NADH 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 a menaquinone. 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. (476 aa)
SKC85523.1NADH-quinone oxidoreductase subunit M. (515 aa)
SKC85527.1NADH-quinone oxidoreductase subunit L. (628 aa)
nuoK-3NADH-quinone oxidoreductase 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 a menaquinone. 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)
SKC85534.1NADH 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. (173 aa)
nuoI-2NADH 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. (171 aa)
nuoH-3NADH 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. (315 aa)
SKC85544.1NADH dehydrogenase subunit G; Belongs to the complex I 75 kDa subunit family. (912 aa)
SKC85549.1NADH 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. (440 aa)
SKC85551.1NADH dehydrogenase subunit E. (154 aa)
nuoD-3NADH-quinone oxidoreductase subunit C/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 a menaquinone. 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. In the N-terminal section; belongs to the complex I 30 kDa subunit family. (579 aa)
nuoB-3NADH dehydrogenase subunit B; 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 a menaquinone. 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. (212 aa)
nuoA-3NADH 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 a menaquinone. 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. (142 aa)
SKC85741.1Predicted Zn-dependent peptidase. (993 aa)
SKC86063.1Starch-binding associating with outer membrane. (532 aa)
SKC86113.1Starch-binding associating with outer membrane. (536 aa)
SKC86275.1Cytochrome C oxidase subunit IV. (110 aa)
Your Current Organism:
Ohtaekwangia koreensis
NCBI taxonomy Id: 688867
Other names: Bacteroidetes bacterium 3B-2, CCUG 58939, DSM 25262, KCTC 23018, O. koreensis, Ohtaekwangia koreensis Yoon et al. 2011, strain 3B-2
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