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3.D.2.2.2
H+-transporting NADH/NADP Transhydrogenase, PntA1 (α1)/PntA2 (α2)/PntB (β).  A 3-d structure is available (Leung et al. 2015). Another structre (2.2 Å resolution) revealed conformational changes of helix positions from the previous structure solved at pH 8.5, and  internal water molecules interacting with residues implicated in proton translocation. Water flows across a narrow pore and a hydrophobic "dry" region in the middle of the membrane channel, with key residues His42alpha2 (chain A) being protonated and Thr214beta (chain B) displaying a conformational change, respectively, to gate the channel access to both cytoplasmic and periplasmic chambers. Mutation of Thr214beta to Ala deactivated the enzyme (Padayatti et al. 2017).

Accession Number:Q72GR8
Protein Name:NAD/NADP transhydrogenase alpha subunit 1
Length:375
Molecular Weight:39972.00
Species:Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [262724]
Number of TMSs:2
Substrate hydron

Cross database links:

Structure:
4IZH   4IZI   4J16   4J1T   4O9U     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MVTVAVPKER APGERRVALV PEVVARLVKG GARVRVERGA GEGAYHPDEA YQEAGAEVVE 
61:	RGELLKGAHL LFTVQPPPED LIQALEPGAI VVGFVQPHKN LELVRALQAK KATVIAMELI 
121:	PRITRAQSMD ALSSQATVAG YLAAIHAARL SPRFFPMLTT AAGTIRPAKV MVMGVGVAGL 
181:	MAIATAKRLG AQVFAYDVRK AALEQALSLG AKPIELPISA EGEGGYAREL TEEEKRIQHE 
241:	ALRDHVAGMD VLITTAQVPG RRAPILLTED MVERLKPGTV VVDLAAESGG NCVLTKPGEV 
301:	VEVRGVRVYG PLNLPSELSV HASEMYAKNL YNLSSLLIEK GAFAPKWEDE IVRAALLMKE 
361:	GEVLHGPTKA LLGGA