InterPro : IPR016161

Name  Aldehyde/histidinol dehydrogenase Short Name  Ald_DH/histidinol_DH
Type  Domain Description  This entry represents a structural domain found in aldehyde dehydrogenases []and histidinol dehydrogenases []. These proteins contain two similar domains, each with a 3-layer alpha/beta/alpha structure, which probably arose from a duplication. These enzymes bind NAD differently from other NAD(P)-dependent oxidoreductases. Aldehyde dehydrogenases (and ) are enzymes that oxidize a wide variety of aliphatic and aromatic aldehydes using NADP as a cofactor. In mammals at least four different forms of the enzyme are known []: class-1 (or Ald C) a tetrameric cytosolic enzyme, class-2 (or Ald M) a tetrameric mitochondrial enzyme, class- 3 (or Ald D) a dimeric cytosolic enzyme, and class IV a microsomal enzyme. Aldehyde dehydrogenases have also been sequenced from fungal and bacterial species. A number of enzymes are known to be evolutionary related to aldehyde dehydrogenases. A glutamic acid and a cysteine residue have been implicated in the catalytic activity of mammalian aldehyde dehydrogenase.Histidinol dehydrogenase () (HDH) catalyses the terminal step in the biosynthesis of histidine in bacteria, fungi, and plants, the four-electron oxidation of L-histidinol to histidine. In 4-electron dehydrogenases, a single active site catalyses 2 separate oxidation steps: oxidation of the substrate alcohol to an intermediate aldehyde; and oxidation of the aldehyde to the product acid, in this case His []. The reaction proceeds via a tightly- or covalently-bound inter-mediate, and requires the presence of 2 NAD molecules []. By contrast with most dehydrogenases, the substrate is bound before the NAD coenzyme []. A Cys residue has been implicated in the catalytic mechanism of the second oxidative step []. In bacteria HDH is a single chain polypeptide; in fungi it is the C-terminal domain of a multifunctional enzyme which catalyzes three different steps of histidine biosynthesis; and in plants it is expressed as nuclear encoded protein precursor which is exported to the chloroplast [].
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

1 Child Features

Id Name Short Name Type
IPR015590 Aldehyde dehydrogenase domain Aldehyde_DH_dom Domain

5 Contains

Id Name Short Name Type
IPR016163 Aldehyde dehydrogenase, C-terminal Ald_DH_C Domain
IPR016162 Aldehyde dehydrogenase N-terminal domain Ald_DH_N Domain
IPR020593 Gamma-glutamyl phosphate reductase GPR, conserved site G-glutamylP_reductase_CS Conserved_site
IPR016160 Aldehyde dehydrogenase, cysteine active site Ald_DH_CS_CYS Conserved_site
IPR001692 Histidinol dehydrogenase, conserved site Histidinol_DH_CS Conserved_site

2 Found In

Id Name Short Name Type
IPR017649 Succinylglutamic semialdehyde dehydrogenase SuccinylGlu_semiald_DH_AstD Family
IPR008670 Acyl-CoA reductase, LuxC Acyl-CoA_reduct_LuxC Family

0 Parent Features

5 Publications

First Author Title Year Journal Volume Pages
Grubmeyer CT A cysteine residue (cysteine-116) in the histidinol binding site of histidinol dehydrogenase. 1986 Biochemistry 25 4778-84
Nagai A Structural and functional conservation of histidinol dehydrogenase between plants and microbes. 1991 Proc Natl Acad Sci U S A 88 4133-7
Hempel J Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated liver: distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitochondria. 1989 Biochemistry 28 1160-7
Barbosa JA Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase. 2002 Proc Natl Acad Sci U S A 99 1859-64
Perez-Miller SJ Coenzyme isomerization is integral to catalysis in aldehyde dehydrogenase. 2003 Biochemistry 42 7100-9



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)