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InterPro: IPR010097 Malate dehydrogenase, NAD-dependent, eukaryote/gamma proteobacteria

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UniProtKB

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1888 proteins

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Accession List
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Accession

IPR010097 Malate_DH_NAD-dep_euk/g-bac

Type

Family

Signatures Help

Database	ID	Name	Proteins
PANTHER	PTHR11540:SF1	MDH_euk_g_bac	1881
TIGRFAMs	TIGR01772	MDH_euk_gproteo	1044
Signatures in BioMart

InterPro Relationships Help

Parent

IPR001236 Lactate/malate dehydrogenase

Contains

IPR001252 Malate dehydrogenase, active site
IPR015955 Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal
IPR016040 NAD(P)-binding domain

GO Term annotation Help

Process

GO:0006108 malate metabolic process
GO:0055114 oxidation reduction

Function

GO:0030060 L-malate dehydrogenase activity

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents the NAD-dependent malate dehydrogenase found in eukaryotes and certain gamma proteobacteria. The enzyme is involved in the citric acid cycle as well as the glyoxalate cycle. Several isoforms exist in eukaryotes. In Saccharomyces cereviseae, for example, there are cytoplasmic, mitochondrial and peroxisomal forms. Although malate dehydrogenases have in some cases been mistaken for lactate dehydrogenases due to the similarity of these two substrates and the apparent ease with which evolution can toggle these activities, critical residues have been identified [1] which can discriminate between the two activities.

Structural links Help

PDB - click here

SCOP: c.2.1.5 , d.162.1.1

CATH: 3.40.50.720 , 3.90.110.10

Database links Help

Enzyme: EC:1.1.1.37

CluSTr: ALLvsALL:437:41.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR010097

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O02640 Probable malate dehydrogenase, mitochondrial

O82399 Probable malate dehydrogenase, glyoxysomal

P08249 Malate dehydrogenase, mitochondrial

P17505 Malate dehydrogenase, mitochondrial

P40926 Malate dehydrogenase, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001236	Lactate/malate dehydrogenase
IPR010097	Malate dehydrogenase, NAD-dependent, eukaryote/gamma proteobacteria
IPR016040	NAD(P)-binding domain
IPR001252	Malate dehydrogenase, active site
IPR001557	L-lactate/malate dehydrogenase
IPR015955	Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain

Publications Open in usermanual
1.	Hannenhalli SS, Russell RB. Analysis and prediction of functional sub-types from protein sequence alignments. J. Mol. Biol. 303 61-76 2000 [PubMed: 11021970] http://dx.doi.org/10.1006/jmbi.2000.4036

Additional Reading Open in usermanual
	Gleason WB, Fu Z, Birktoft J, Banaszak L. Refined crystal structure of mitochondrial malate dehydrogenase from porcine heart and the consensus structure for dicarboxylic acid oxidoreductases. Biochemistry 33 1994 2078-88 [PubMed: 8117664] http://dx.doi.org/10.1021/bi00174a014
	Hall MD, Banaszak LJ. Crystal structure of a ternary complex of Escherichia coli malate dehydrogenase citrate and NAD at 1.9 A resolution. J. Mol. Biol. 232 1993 213-22 [PubMed: 8331658] http://dx.doi.org/10.1006/jmbi.1993.1377
	Hall MD, Levitt DG, Banaszak LJ. Crystal structure of Escherichia coli malate dehydrogenase. A complex of the apoenzyme and citrate at 1.87 A resolution. J. Mol. Biol. 226 1992 867-82 [PubMed: 1507230] http://dx.doi.org/10.1016/0022-2836(92)90637-Y
	Cox B, Chit MM, Weaver T, Gietl C, Bailey J, Bell E, Banaszak L. Organelle and translocatable forms of glyoxysomal malate dehydrogenase. The effect of the N-terminal presequence. FEBS J. 272 2005 643-54 [PubMed: 15670147] http://dx.doi.org/10.1111/j.1742-4658.2004.04475.x
	Bell JK, Yennawar HP, Wright SK, Thompson JR, Viola RE, Banaszak LJ. Structural analyses of a malate dehydrogenase with a variable active site. J. Biol. Chem. 276 2001 31156-62 [PubMed: 11389141] http://dx.doi.org/10.1074/jbc.M100902200

InterPro 23.1