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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:Q8DMR6
Protein Name:NAD(P)H-quinone oxidoreductase subunit 2
Length:515
Molecular Weight:55144.00
Species:Thermosynechococcus elongatus (strain BP-1) [197221]
Number of TMSs:14
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:	MDLVTLAGQL NAGTILPETI LIVTLLVVLL ADLIQGRQAD RWTPYFAIVG LGGAIATMIP 
61:	LWTQPATISF FGSFISDHLS LFFRGLIALS ALGTILMSIR YVEQTGSSLG EFMTILLTAT 
121:	VGGMFIAGAQ ELVFIFVALE TLSIASYLLT GYTKRDSRSN EAALKYLLIG AASSAIFLYG 
181:	SSLLYGLSGG HTQLPAIAQA LSSESLGLVV ALVFVIAGIS FKISAVPFHQ WTPDVYEGAP 
241:	TPVVAFLSVG SKAAGFALAI RFLTLAFPSV TDQWQLIFTV LAILSMILGN VVALAQTSMK 
301:	RMLAYSSIGQ AGFVMIGFVV GTEAGYASML FYLLVYLFMN LGAFTCVILF SLRTGTDQIS 
361:	EYAGLYQKDP LLTLGLSLCL LSLGGIPPLA GFFGKIYLFW AGWQAGAYGL VLLGLLTSVI 
421:	SIYYYIRVVK MMVVKEPQEM SEAVRNYPEV SWSSFGLRPL QVGLVMTVIA TSLAGILANP 
481:	LFNLVNTAVW DVPQLANQPT VMEVAYQALS PAGKS