malic Malic enzyme, N-terminal domain
SMART ACC:	SM001274
Description:	-
InterPro ACC:	IPR012301
InterPro abstract:	This entry represents the N-terminal domain of the NAD(P)-dependent malic enzyme and related proteins from bacteria, eukaryotes and archaea. Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate, a reaction important in a number of metabolic pathways - e.g. carbon dioxide released from the reaction may be used in sugar production during … expand This entry represents the N-terminal domain of the NAD(P)-dependent malic enzyme and related proteins from bacteria, eukaryotes and archaea. Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate, a reaction important in a number of metabolic pathways - e.g. carbon dioxide released from the reaction may be used in sugar production during the Calvin cycle of photosynthesis [ PUBMED:8300616 ]. There are 3 forms of the enzyme [ PUBMED:1993674 ]: an NAD-dependent form that decarboxylates oxaloacetate; an NAD-dependent form that does not decarboxylate oxalo-acetate; and an NADPH-dependent form [ PUBMED:8300616 ]. Other proteins known to be similar to malic enzymes are the Escherichia coli scfA protein; an enzyme from Zea mays (Maize), formerly thought to be cinnamyl-alcohol dehydrogenase [ PUBMED:2103472 ]; and the hypothetical Saccharomyces cerevisiae protein YKL029c. Studies on the duck liver malic enzyme reveals that it can be alkylated by bromopyruvate, resulting in the loss of oxidative decarboxylation and the subsequent enhancement of pyruvate reductase activity [ PUBMED:1911848 ]. The alkylated form is able to bind NADPH but not L-malate, indicating impaired substrate or divalent metal ion-binding in the active site [ PUBMED:1911848 ]. Sequence analysis has highlighted a cysteine residue as the point of alkylation, suggesting that it may play an important role in the activity of the enzyme [ PUBMED:1911848 ], although it is absent in the sequences from some species. Malic enzyme is a tetramer comprised of subunits with four domains each [ PUBMED:10477256 PUBMED:12033925 PUBMED:1640469 ]. collapse
GO function:	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616), malic enzyme activity (GO:0004470)
Family alignment:	View the Family alignment or the Alignment consensus sequence
There are 30 325 malic domains in 30 291 proteins in SMART's NRDB database.

Taxonomic distribution of proteins containing malic domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing malic domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

KEGG pathways involving proteins which contain this domain

This information is based on the mapping of SMART genomic protein database to KEGG orthologous groups. Percentages are related to the number of proteins containing a malic domain which could be assigned to a KEGG orthologous group, and not all proteins containing malic domains. Please note that proteins can be included in multiple pathways, ie. the numbers below will not add to 100%.

KEGG pathways

Some of these pathways are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

KEGG orthologous groups

Some of these KOs are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

3D structures in PDB containing this domain

Links to other resources describing this domain

Pfam	malic
InterPro	IPR012301