InterPro : IPR007698

Name  Alanine dehydrogenase/pyridine nucleotide transhydrogenase, NAD(H)-binding domain Short Name  AlaDH/PNT_NAD(H)-bd
Type  Domain Description  Alanine dehydrogenase catalyses the NAD-dependent reversible reductive amination of pyruvate into alanine. Pyridine nucleotide transhydrogenase catalyses the reduction of NADP+to NADPH with the concomitant oxidation of NADH to NAD+. This enzyme is locatedin the plasma membrane of prokaryotes and in the inner membrane of the mitochondria of eukaryotes. The transhydrogenation between NADH and NADP is coupled with the translocation of a proton across the membrane. In prokaryotes the enzyme is composed of two different subunits, an alpha chain (gene pntA)and a beta chain (gene pntB), while in eukaryotes it is a single chain protein.The sequence of alanine dehydrogenase from several bacterial species is related with that of the alpha subunit of bacterial pyridine nucleotide transhydrogenase and the N-terminal half of the eukaryotic enzyme. The two mostconserved regions correspond respectively to the N-terminal domain of these proteins, and to a central glycine-rich region which is part of the NAD(H)-binding site []. This entry represents a domain found in alanine dehydrogenase and pyridine nucleotide transhydrogenase, containing the glycine-rich region. This domain is also found in lysine 2-oxoglutarate reductases [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

1 Contains

Id Name Short Name Type
IPR008143 Alanine dehydrogenase/pyridine nucleotide transhydrogenase, conserved site-2 Ala_DH/PNT_CS2 Conserved_site

1 Found In

Id Name Short Name Type
IPR008141 Alanine dehydrogenase Ala_DH Family

0 Parent Features

2 Publications

First Author Title Year Journal Volume Pages
Delforge D Similarities between alanine dehydrogenase and the N-terminal part of pyridine nucleotide transhydrogenase and their possible implication in the virulence mechanism of Mycobacterium tuberculosis. 1993 Biochem Biophys Res Commun 190 1073-9
Azevedo RA Lysine metabolism in higher plants. 2001 Amino Acids 20 261-79

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)