STRINGSTRING
Acel_0266 Acel_0266 nuoA nuoA nuoB nuoB nuoC nuoC nuoD nuoD Acel_0271 Acel_0271 Acel_0272 Acel_0272 Acel_0273 Acel_0273 nuoH nuoH nuoI nuoI Acel_0276 Acel_0276 nuoK nuoK Acel_0278 Acel_0278 Acel_0279 Acel_0279 nuoN nuoN Acel_0490 Acel_0490 Acel_0956 Acel_0956 Acel_0957 Acel_0957 Acel_0958 Acel_0958 Acel_0961 Acel_0961 Acel_0962 Acel_0962 Acel_0963 Acel_0963 Acel_0964 Acel_0964 Acel_0965 Acel_0965 ctaB ctaB Acel_1507 Acel_1507 Acel_1781 Acel_1781
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:
Acel_0266TIGRFAM: geranylgeranyl reductase; PFAM: monooxygenase, FAD-binding; FAD dependent oxidoreductase; tryptophan halogenase; Lycopene beta and epsilon cyclase; KEGG: fra:Francci3_0537 geranylgeranyl reductase. (445 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 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)
nuoBNADH 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)
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 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. (192 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. (440 aa)
Acel_0271TIGRFAM: NADH-quinone oxidoreductase, E subunit; PFAM: NADH dehydrogenase (ubiquinone), 24 kDa subunit; KEGG: sco:SCO4566 NADH dehydrogenase I chain E. (269 aa)
Acel_0272NADH 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. (434 aa)
Acel_0273NADH 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. (830 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. (451 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. (199 aa)
Acel_0276NADH 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. (275 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 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)
Acel_0278KEGG: sma:SAV4848 putative NADH dehydrogenase chain L; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH-Ubiquinone oxidoreductase (complex I), chain 5/L domain protein; NADH/Ubiquinone/plastoquinone (complex I). (634 aa)
Acel_0279NADH dehydrogenase subunit M; KEGG: tfu:Tfu_2683 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (507 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 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. (519 aa)
Acel_0490Cytochrome-c oxidase; 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. (589 aa)
Acel_0956Cytochrome c oxidase, subunit II; 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). (280 aa)
Acel_0957Cytochrome-c oxidase; 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. (570 aa)
Acel_0958Putative integral membrane protein; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family. (132 aa)
Acel_0961PFAM: Cytochrome b/b6, N-terminal domain; KEGG: tfu:Tfu_1019 ubiquinol-cytochrome c reductase, cytochrome b subunit. (568 aa)
Acel_0962Menaquinol-cytochrome c reductase iron-sulfur subunit precursor; PFAM: Rieske [2Fe-2S] domain protein; KEGG: sco:SCO2149 Rieske iron-sulfur protein. (330 aa)
Acel_0963Menaquinol-cytochrome c reductase cytochrome c1 subunit precursor; PFAM: cytochrome c, class I; KEGG: sco:SCO2150 cytochrome C heme-binding subunit. (268 aa)
Acel_0964PFAM: cytochrome c oxidase, subunit III; KEGG: fra:Francci3_3108 heme/copper-type cytochrome/quinol oxidase subunit 3-like. (223 aa)
Acel_0965KEGG: tfu:Tfu_1023 putative response regulator. (135 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. (307 aa)
Acel_1507PFAM: peptidase M16 domain protein; KEGG: sco:SCO5738 putative protease; Belongs to the peptidase M16 family. (451 aa)
Acel_1781Hypothetical protein; KEGG: gsu:GSU1649 cytochrome b/b6. (611 aa)
Your Current Organism:
Acidothermus cellulolyticus
NCBI taxonomy Id: 351607
Other names: A. cellulolyticus 11B, Acidothermus cellulolyticus 11B, Acidothermus cellulolyticus str. 11B, Acidothermus cellulolyticus strain 11B
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.