STRINGSTRING
ANP51756.1 ANP51756.1 ANP51524.1 ANP51524.1 ANP51523.1 ANP51523.1 azoR azoR ANP56618.1 ANP56618.1 ANP51426.1 ANP51426.1 ANP51422.1 ANP51422.1 ANP51421.1 ANP51421.1 ANP51220.1 ANP51220.1 ANP51219.1 ANP51219.1 ANP51204.1 ANP51204.1 AVL59_17660 AVL59_17660 ANP56572.1 ANP56572.1 ANP50975.1 ANP50975.1 ANP50871.1 ANP50871.1 ANP50117.1 ANP50117.1 ANP50008.1 ANP50008.1 ANP49269.1 ANP49269.1 ANP49233.1 ANP49233.1 ANP49032.1 ANP49032.1 ANP49029.1 ANP49029.1 ANP48984.1 ANP48984.1 nuoN-2 nuoN-2 ANP48836.1 ANP48836.1 ANP48835.1 ANP48835.1 nuoK-2 nuoK-2 ANP48833.1 ANP48833.1 ANP48830.1 ANP48830.1 nuoB-2 nuoB-2 ANP48828.1 ANP48828.1 nuoN nuoN ANP48799.1 ANP48799.1 ANP48798.1 ANP48798.1 nuoK nuoK ANP48796.1 ANP48796.1 ANP48793.1 ANP48793.1 ANP48792.1 ANP48792.1 nuoD-2 nuoD-2 nuoC nuoC nuoB nuoB nuoA nuoA ANP48695.1 ANP48695.1 nuoD nuoD ANP48172.1 ANP48172.1 ANP56146.1 ANP56146.1 azoR-4 azoR-4 azoR-3 azoR-3 ANP55844.1 ANP55844.1 ANP55027.1 ANP55027.1 ANP55020.1 ANP55020.1 ANP55012.1 ANP55012.1 ANP54983.1 ANP54983.1 ANP57080.1 ANP57080.1 ANP54856.1 ANP54856.1 ANP54733.1 ANP54733.1 ANP54582.1 ANP54582.1 ANP54581.1 ANP54581.1 ANP54580.1 ANP54580.1 ANP54577.1 ANP54577.1 ANP54576.1 ANP54576.1 ANP54574.1 ANP54574.1 ANP54376.1 ANP54376.1 ANP54099.1 ANP54099.1 ANP54059.1 ANP54059.1 ANP53782.1 ANP53782.1 ANP56919.1 ANP56919.1 ANP53205.1 ANP53205.1 AVL59_29995 AVL59_29995 ANP52963.1 ANP52963.1 ANP52430.1 ANP52430.1 azoR-2 azoR-2 ANP51698.1 ANP51698.1
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.
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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:
ANP51756.1Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (64 aa)
ANP51524.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (63 aa)
ANP51523.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (427 aa)
azoRFMN-dependent NADH-azoreductase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity; Belongs to the azoreductase type 1 family. (216 aa)
ANP56618.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (317 aa)
ANP51426.1Cytochrome BD ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (488 aa)
ANP51422.1Ferredoxin reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (463 aa)
ANP51421.1Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (75 aa)
ANP51220.1Cytochrome 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. (541 aa)
ANP51219.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (112 aa)
ANP51204.1Cytochrome 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. (554 aa)
AVL59_17660Ubiquinol-cytochrome c reductase cytochrome b subunit; Incomplete; partial on complete genome; missing stop; Derived by automated computational analysis using gene prediction method: Protein Homology. (127 aa)
ANP56572.1Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (66 aa)
ANP50975.1Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (249 aa)
ANP50871.1Proline dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (100 aa)
ANP50117.1Ferredoxin; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (108 aa)
ANP50008.1Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (72 aa)
ANP49269.1Ferredoxin; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (106 aa)
ANP49233.1Succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. (256 aa)
ANP49032.1Succinate dehydrogenase, cytochrome b556 subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. (114 aa)
ANP49029.1Succinate dehydrogenase iron-sulfur subunit; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (253 aa)
ANP48984.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (627 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. (507 aa)
ANP48836.1NADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (524 aa)
ANP48835.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (673 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. (126 aa)
ANP48833.1NADH dehydrogenase; 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. (203 aa)
ANP48830.1Dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (426 aa)
nuoB-2Hydroxyacid dehydrogenase; 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. (228 aa)
ANP48828.1NADH-quinone oxidoreductase subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. (138 aa)
nuoNNADH:ubiquinone 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. (549 aa)
ANP48799.1NADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (523 aa)
ANP48798.1NADH-quinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. (631 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. (99 aa)
ANP48796.1NADH:ubiquinone 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. (280 aa)
ANP48793.1NADH-quinone oxidoreductase 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. (834 aa)
ANP48792.1NADH oxidoreductase (quinone) 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. (447 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. (446 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. (254 aa)
nuoBNADH dehydrogenase; 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)
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. (119 aa)
ANP48695.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (242 aa)
nuoDNADH-quinone oxidoreductase 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. (382 aa)
ANP48172.1Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (62 aa)
ANP56146.1Cytochrome BD ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (502 aa)
azoR-4FMN-dependent NADH-azoreductase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity; Belongs to the azoreductase type 1 family. (216 aa)
azoR-3FMN-dependent NADH-azoreductase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity; Belongs to the azoreductase type 1 family. (216 aa)
ANP55844.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (376 aa)
ANP55027.1Ferredoxin reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (50 aa)
ANP55020.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (203 aa)
ANP55012.1Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (75 aa)
ANP54983.1Oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (536 aa)
ANP57080.14Fe-4S ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (121 aa)
ANP54856.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (101 aa)
ANP54733.1Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (77 aa)
ANP54582.1Cytochrome c oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (319 aa)
ANP54581.1Cytochrome 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. (577 aa)
ANP54580.1Cytochrome C oxidase subunit IV; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family. (132 aa)
ANP54577.1Derived by automated computational analysis using gene prediction method: Protein Homology. (206 aa)
ANP54576.1Cystathionine beta-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. (270 aa)
ANP54574.1Ubiquinol-cytochrome c reductase cytochrome b subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. (543 aa)
ANP54376.1FeS-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (144 aa)
ANP54099.1Formate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (208 aa)
ANP54059.1Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (100 aa)
ANP53782.1Photosystem reaction center subunit H; Derived by automated computational analysis using gene prediction method: Protein Homology. (122 aa)
ANP56919.1Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (80 aa)
ANP53205.1Electron transfer flavoprotein subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology. (261 aa)
AVL59_29995Endonuclease; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. (320 aa)
ANP52963.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (221 aa)
ANP52430.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (221 aa)
azoR-2FMN-dependent NADH-azoreductase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity; Belongs to the azoreductase type 1 family. (212 aa)
ANP51698.1Amidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (98 aa)
Your Current Organism:
Streptomyces griseochromogenes
NCBI taxonomy Id: 68214
Other names: ATCC 14511, BCRC 11818, CBS 714.72, CCRC 11818, CCRC:11818, DSM 40499, IFO 13413, ISP 5499, JCM 4039, JCM 4764, KCTC 9027, NBRC 13413, NRRL B-12423, NRRL-ISP 5499, S. griseochromogenes, Streptomyces griseichromogenes
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