STRINGSTRING
ndhB ndhB ndhL ndhL AII44963.1 AII44963.1 AII45764.1 AII45764.1 AII46242.1 AII46242.1 ndhO ndhO ndhM ndhM AII46307.1 AII46307.1 ndhD ndhD ndhE ndhE AII46317.1 AII46317.1 ndhI ndhI ndhA ndhA ndhH ndhH AII46710.1 AII46710.1 ndhC ndhC ndhK ndhK ndhJ ndhJ ndhN ndhN AII47287.1 AII47287.1 AII47288.1 AII47288.1
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.
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:
ndhBOxidoreductase; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (523 aa)
ndhLNAD(P)H-quinone oxidoreductase subunit L; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (85 aa)
AII44963.1NAD(P)H-quinone oxidoreductase subunit 4; Shuttles electrons from NAD(P)H, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain; subunit D, with NdhB and NdhF are core membrane components; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (523 aa)
AII45764.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (182 aa)
AII46242.1Thioredoxin; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (310 aa)
ndhONAD(P)H-quinone oxidoreductase subunit O; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (87 aa)
ndhMNAD(P)H-quinone oxidoreductase subunit M; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (115 aa)
AII46307.1Oxidoreductase; Catalyzes the transfer of electrons from NADH to ubiquinone; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (670 aa)
ndhDNAD(P)H-quinone oxidoreductase subunit 4; NDH-1 shuttles electrons from NAD(P)H, 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 plastoquinone. 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 4 family. (551 aa)
ndhENADH:ubiquinone oxidoreductase subunit K; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (109 aa)
AII46317.1NADH: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. Belongs to the complex I subunit 6 family. (201 aa)
ndhINADH dehydrogenase subunit I; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient; Belongs to the complex I 23 kDa subunit family. (212 aa)
ndhANADPH-quinone oxidoreductase; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. (373 aa)
ndhHNADPH-quinone oxidoreductase; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (394 aa)
AII46710.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (61 aa)
ndhCNADPH-quinone oxidoreductase; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (120 aa)
ndhKNADH dehydrogenase subunit B; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration; Belongs to the complex I 20 kDa subunit family. (251 aa)
ndhJNADH dehydrogenase subunit J; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (159 aa)
ndhNNAD(P)H-quinone oxidoreductase subunit N; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (153 aa)
AII47287.1Oxidoreductase; Catalyzes the transfer of electrons from NADH to ubiquinone; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (614 aa)
AII47288.1NAD(P)H-quinone oxidoreductase subunit D4; Catalyzes the transfer of electrons from NADH to ubiquinone; NdhD4 is possibly involved in a constitutive CO(2)-uptake system; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (496 aa)
Your Current Organism:
Synechococcus sp. KORDI49
NCBI taxonomy Id: 585423
Other names: S. sp. KORDI-49, Synechococcus sp. KORDI-49
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.