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SDY_0920 SDY_0920 ydbK ydbK acpP acpP SDY_2391 SDY_2391 nuoN nuoN nuoM nuoM nuoL nuoL nuoK nuoK nuoJ nuoJ nuoI nuoI nuoH nuoH nuoG nuoG nuoF nuoF nuoE nuoE nuoC nuoC nuoB nuoB nuoA nuoA yffG yffG hyfA hyfA hyfB hyfB hyfC hyfC hyfE hyfE hyfF hyfF hyfG hyfG hyfI hyfI yfhL yfhL hycI hycI hycH hycH hycF hycF hycE hycE hycD hycD hycB hycB yraR yraR yiaI yiaI yhjJ yhjJ
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:
SDY_0920Conserved hypothetical protein; Code: R; COG: COG3217; orf. (369 aa)
ydbKPutative oxidoreductase, Fe-S subunit; Code: C; COG: COG0674. (1174 aa)
acpPAcyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family. (78 aa)
SDY_2391Putative enzyme; Code: C; COG: COG1018. (322 aa)
nuoNNADH dehydrogenase I chain 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. (425 aa)
nuoMNADH dehydrogenase I chain M; Code: C; COG: COG1008. (509 aa)
nuoLNADH dehydrogenase I chain L; Code: CP; COG: COG1009. (613 aa)
nuoKNADH dehydrogenase I chain 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. (100 aa)
nuoJNADH dehydrogenase I chain 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. (184 aa)
nuoINADH dehydrogenase I chain 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. (180 aa)
nuoHNADH dehydrogenase I chain 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. (325 aa)
nuoGNADH dehydrogenase I chain 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. (910 aa)
nuoFNADH dehydrogenase I chain 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. (445 aa)
nuoENADH dehydrogenase I chain E; Code: C; COG: COG1905. (166 aa)
nuoCNADH dehydrogenase I chain 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 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; In the N-terminal section; belongs to the complex I 30 kDa subunit family. (600 aa)
nuoBNADH dehydrogenase I chain 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 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. (220 aa)
nuoANADH dehydrogenase I chain 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. (147 aa)
yffGPutative oxidoreductase, Fe-S subunit; Code: ER; COG: COG0493. (659 aa)
hyfAHydrogenase 4 Fe-S subunit; Code: C; COG: COG1142. (218 aa)
hyfBHydrogenase 4 membrane subunit; Code: CP; COG: COG0651. (672 aa)
hyfCHydrogenase 4 membrane subunit; Code: C; COG: COG0650. (322 aa)
hyfEHydrogenase 4 membrane subunit; Code: C; COG: COG4237. (216 aa)
hyfFHydrogenase 4 membrane subunit; Code: CP; COG: COG0651. (526 aa)
hyfGHydrogenase 4 subunit; Code: C; COG: COG3261. (571 aa)
hyfIHydrogenase 4 Fe-S subunit; Code: C; COG: COG3260. (252 aa)
yfhLConserved hypothetical protein; Code: C; COG: COG1145; orf. (86 aa)
hycIHycI; Protease involved in processing C-terminal end of the large subunit of hydrogenase 3; Code: C; COG: COG0680. (155 aa)
hycHHycH; Processing of large subunit (HycE) of hydrogenase 3 (part of the FHL complex). (136 aa)
hycFProbable iron-sulfur protein of hydrogenase 3; Part of FHL complex; Code: C; COG: COG1143. (180 aa)
hycELarge subunit of hydrogenase 3; Part of FHL complex; Code: C; COG: COG3261. (569 aa)
hycDMembrane-spanning protein of hydrogenase 3; Part of FHL complex; Code: C; COG: COG0650. (269 aa)
hycBProbable small subunit of hydrogenase-3, iron-sulfur protein; Part of formate hydrogenlyase (FHL) complex; Code: C; COG: COG1142. (203 aa)
yraRConserved hypothetical protein; Code: MG; COG: COG0702; orf. (226 aa)
yiaIConserved hypothetical protein; Code: C; COG: COG1142; orf. (157 aa)
yhjJConserved hypothetical protein; Code: R; COG: COG0612; orf. (498 aa)
Your Current Organism:
Shigella dysenteriae
NCBI taxonomy Id: 300267
Other names: S. dysenteriae Sd197, Shigella dysenteriae Sd197, Shigella dysenteriae str. Sd197, Shigella dysenteriae strain Sd197
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