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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:Q72GS0
Protein Name:NAD(P) transhydrogenase subunit beta
Length:450
Molecular Weight:47336.00
Species:Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [262724]
Number of TMSs:9
Substrate hydron

Cross database links:

Structure:
4J16   4J1T   4O93   4O9P   4O9T   4O9U   5UNI     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MDLIQAAYFV VAILFIVGLK RMAHPTTAKS GIVWAGWGMV LAVLATFFWP GMGNFALILL 
61:	ALLLGSVVAW WAAVRVAMTD MPQMVAIYNG MGGGAAATIA AVELLKGAFE NTGLMALAIL 
121:	GGLIGSVAFT GSLIAFAKLQ GIMKSRPILF PGQKAVNALV LALTVVIGLS LLWNDATASI 
181:	VLFFLLALLF GVLMTLPIGG GDMPVAISFY NAFTGMAVGF EGFAVGNPAL MVAGTLVGAA 
241:	GTLLTVLMAR AMNRSVWSVL VGGFGVEQEA GEVKGSLKPI DVEDAAVMLA YAGKVVFVPG 
301:	YGMALSQAQH KLKELADLLE ARGVEVKFAI HPVAGRMPGH MNVLLAEAGV DYDKLKDLEE 
361:	INPEFPTVDV AVVIGANDVV NPAARRPGSP LYGMPILDVD KAKNVIVIKR GQGKGFAGVE 
421:	NELFYAENTR MLYGDAQKVL TELIQALKRL