InterPro : IPR008143

Name  Alanine dehydrogenase/pyridine nucleotide transhydrogenase, conserved site-2 Short Name  Ala_DH/PNT_CS2
Type  Conserved_site Description  Alanine dehydrogenases () and pyridine nucleotide transhydrogenase () have beenshown to share regions of similarity []. Alanine dehydrogenase catalyzes the NAD-dependentreversible reductive amination of pyruvate into alanine. Pyridine nucleotide transhydrogenase catalyzesthe 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. Thetranshydrogenation between NADH and NADP is coupled with the translocation of a proton across themembrane. 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 alaninedehydrogenase from several bacterial species are related with those of the alpha subunit of bacterialpyridine nucleotide transhydrogenase and of the N-terminal half of the eukaryotic enzyme. The two mostconserved regions correspond respectively to the N-terminal extremity of these proteins and to a centralglycine-rich region which is part of the NAD(H)-binding site.This signature corresponds to the central glycine-rich region which is part of theNAD(H)-binding site, it is found in alanine dehydrogenases () and also in the lysine 2-oxoglutarate reductases.
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

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0 Contains

3 Found In

Id Name Short Name Type
IPR016040 NAD(P)-binding domain NAD(P)-bd_dom Domain
IPR007698 Alanine dehydrogenase/pyridine nucleotide transhydrogenase, NAD(H)-binding domain AlaDH/PNT_NAD(H)-bd Domain
IPR008141 Alanine dehydrogenase Ala_DH Family

0 Parent Features

1 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



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)