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3.D.1.8.2
The photosynthetic/respiratory NAD(P)H-quinone oxidoreductase subunits A - Q and S. NdhP and NdhQ are peptides of 42 and 39 aas, identified by cryoEM at 3.3 Å resolution (Schuller et al. 2019). NDH-1 (NdhA) shuttles electrons from reduced ferridoxin, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and photosynthetic chains. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. The system couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (Schuller et al. 2019). Ferridoxin directly mediates electron transfer between photosystem I and complex I. Ferridoxin efficiently binds to complex I with subunit NdhS being the key component in this process (Schuller et al. 2019).

Accession Number:Q8DJ02
Protein Name:NAD(P)H-quinone oxidoreductase subunit 3
Length:132
Molecular Weight:15003.00
Species:Thermosynechococcus elongatus (strain BP-1) [197221]
Number of TMSs:3
Location1 / Topology2 / Orientation3: Cellular thylakoid membrane1 / Multi-pass membrane protein2
Substrate proton

Cross database links:

Structure:
6HUM   6KHI   6KHJ   6L7O   6L7P   6NBQ   6NBX   6NBY   6TJV      [...more]

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MVAIPRLRDT ATVFVLSGYE YFLGFLIICS LVPVLALAAS ALLRPKSGRM IRLTTYESGM 
61:	EPIGGAWIQF NVRYYMFALV FVIFDVETVF LYPWAVAFHQ LGLLAFIEAL IFIAILVVAL 
121:	VYAWRKRALE WS