InterPro : IPR015955

Name  Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal Short Name  Lactate_DH/Glyco_Ohase_4_C
Type  Domain Description  This entry represents a structural motif found at the C-terminal of lactate dehydrogenase ()and malate dehydrogenases (), as well as at the C-terminal of family 4 glycoside hydrolases (). These domains have an unusual fold consisting of segregated alpha-helical and beta-sheet regions, although they contain predominantly anti-parallel beta-sheets [, , ].L-lactate dehydrogenases are metabolic enzymes that catalyse the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis. L-lactate dehydrogenase is also found as a lens crystallin in bird and crocodile eyes. Malate dehydrogenases catalyse the interconversion of malate to oxaloacetate. The enzyme participates in the citric acid cycle.O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [, ]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in 'clans'. Glycoside hydrolase family 4 comprises enzymes with several known activities; 6-phospho-beta-glucosidase (); 6-phospho-alpha-glucosidase (); alpha-galactosidase ().
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

2 Child Features

Id Name Short Name Type
IPR022383 Lactate/malate dehydrogenase, C-terminal Lactate/malate_DH_C Domain
IPR022616 Glycosyl hydrolase, family 4, C-terminal Glyco_hydro_4_C Domain

2 Contains

Id Name Short Name Type
IPR001252 Malate dehydrogenase, active site Malate_DH_AS Active_site
IPR018177 L-lactate dehydrogenase, active site L-lactate_DH_AS Active_site

9 Found In

Id Name Short Name Type
IPR001557 L-lactate/malate dehydrogenase L-lactate/malate_DH Family
IPR010945 Malate dehydrogenase, type 2 Malate_DH_type2 Family
IPR010097 Malate dehydrogenase, type 1 Malate_DH_type1 Family
IPR011274 Malate dehydrogenase, NAD-dependent, cytosolic Malate_DH_NAD-dep_euk Family
IPR011304 L-lactate dehydrogenase L-lactate_DH Family
IPR001088 Glycoside hydrolase, family 4 Glyco_hydro_4 Family
IPR011275 Malate dehydrogenase, type 3 Malate_DH_type3 Family
IPR011272 Lactate dehydrogenase, protist Lactate_DH_protist Family
IPR011273 Malate dehydrogenase, NADP-dependent, plants Malate_DH_NADP-dep_pln Family

0 Parent Features

5 Publications

First Author Title Year Journal Volume Pages
Henrissat B Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. 1995 Proc Natl Acad Sci U S A 92 7090-4
Davies G Structures and mechanisms of glycosyl hydrolases. 1995 Structure 3 853-9
Read JA Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase. 2001 Proteins 43 175-85
Gleason WB Refined crystal structure of mitochondrial malate dehydrogenase from porcine heart and the consensus structure for dicarboxylic acid oxidoreductases. 1994 Biochemistry 33 2078-88
Lodge JA Crystal structure of Thermotoga maritima alpha-glucosidase AglA defines a new clan of NAD+-dependent glycosidases. 2003 J Biol Chem 278 19151-8



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)